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Carbohydrate-binding module

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CBM_1
three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase i from trichoderma reesei, nmr, 18 structures
Identifiers
SymbolCBM_1
PfamPF00734
Pfam clanCL0083
ECOD387.1.1
InterProIPR000254
PROSITEPDOC00486
SCOP21cel / SCOPe / SUPFAM
CAZyCBM1
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM_2
solution structure of a cellulose binding domain from cellulomonas fimi by nuclear magnetic resonance spectroscopy
Identifiers
SymbolCBM_2
PfamPF00553
Pfam clanCL0203
ECOD11.1.5
InterProIPR001919
PROSITEPDOC00485
SCOP21exg / SCOPe / SUPFAM
CAZyCBM2
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM_3
crystal structure of a family iiia cbd from clostridium cellulolyticum
Identifiers
SymbolCBM_3
PfamPF00942
Pfam clanCL0203
ECOD11.1.5
InterProIPR001956
SCOP21nbc / SCOPe / SUPFAM
CAZyCBM3
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM_5/12
interactions of a family 18 chitinase with the designed inhibitor hm508, and its degradation product, chitobiono-delta-lactone
Identifiers
SymbolCBM_5_12
PfamPF02839
ECOD64.3.1
InterProIPR003610
SCOP21ed7 / SCOPe / SUPFAM
CAZyCBM12
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM_6
cbm6ct from clostridium thermocellum in complex with xylopentaose
Identifiers
SymbolCBM_6
PfamPF03422
Pfam clanCL0202
ECOD10.32.1
InterProIPR005084
SCOP21gmm / SCOPe / SUPFAM
CAZyCBM6
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM_4/9
cbm4 structure and function
Identifiers
SymbolCBM_4_9
PfamPF02018
Pfam clanCL0202
ECOD10.32.1
InterProIPR003305
SCOP21ulp / SCOPe / SUPFAM
CAZyCBM22
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM_10
solution structure of type x cbm
Identifiers
SymbolCBM_10
PfamPF02013
ECOD908.1.1
InterProIPR002883
SCOP21qld / SCOPe / SUPFAM
CAZyCBM10
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM_11
family 11 carbohydrate-binding module of cellulosomal cellulase lic26a-cel5e of clostridium thermocellum
Identifiers
SymbolCBM_11
PfamPF03425
Pfam clanCL0202
ECOD10.32.1
InterProIPR005087
CAZyCBM11
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM_14
Identifiers
SymbolCBM_14
PfamPF01607
Pfam clanCL0155
ECOD394.1.1
InterProIPR002557
SCOP21dqc / SCOPe / SUPFAM
CAZyCBM14
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM_15
xylan-binding module cbm15
Identifiers
SymbolCBM_15
PfamPF03426
Pfam clanCL0202
ECOD10.32.1
InterProIPR005088
SCOP21gny / SCOPe / SUPFAM
CAZyCBM15
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM_17/28
structure of fam17 carbohydrate binding module from clostridium cellulovorans
Identifiers
SymbolCBM_17_28
PfamPF03424
Pfam clanCL0202
ECOD10.32.1
InterProIPR005086
SCOP21g0c / SCOPe / SUPFAM
CAZyCBM28
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Chitin_bind_1 (CBM18)
crystal structure analysis of crosslinked-wga3/glcnacbeta1,4glcnac complex
Identifiers
SymbolChitin_bind_1
PfamPF00187
ECOD387.1.2
InterProIPR001002
PROSITEPDOC00025
SCOP21wgt / SCOPe / SUPFAM
CAZyCBM18
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM_19
Identifiers
SymbolCBM_19
PfamPF03427
Pfam clanCL0155
InterProIPR005089
CAZyCBM19
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM_20
glucoamylase, granular starch-binding domain complex with cyclodextrin, nmr, minimized average structure
Identifiers
SymbolCBM_20
PfamPF00686
Pfam clanCL0369
ECOD11.1.4
InterProIPR002044
SCOP21cdg / SCOPe / SUPFAM
CAZyCBM20
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM_21
Identifiers
SymbolCBM_21
PfamPF03370
ECOD11.1.1
InterProIPR005036
CAZyCBM21
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM_25
Identifiers
SymbolCBM_25
PfamPF03423
ECOD11.1.4
InterProIPR005085
CAZyCBM25
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM27
structural and thermodynamic dissection of specific mannan recognition by a carbohydrate-binding module, tmcbm27
Identifiers
SymbolCBM27
PfamPF09212
ECOD10.32.1
InterProIPR015295
SCOP21oh4 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Chitin_bind_3 (CBM33)
crystal structure of the serratia marcescens chitin-binding protein cbp21 y54a mutant.
Identifiers
SymbolChitin_bind_3
PfamPF03067
Pfam clanCL0159
ECOD11.1.1
InterProIPR004302
CAZyCBM33
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM_48
crystal structure of glycosyltrehalose trehalohydrolase from sulfolobus solfataricus
Identifiers
SymbolCBM_48
PfamPF02922
Pfam clanCL0369
ECOD11.1.1
InterProIPR004193
SCOP21bf2 / SCOPe / SUPFAM
CAZyCBM48
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CBM49
Identifiers
SymbolCBM49
PfamPF09478
Pfam clanCL0203
InterProIPR019028
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, a carbohydrate-binding module (CBM) is a protein domain found in carbohydrate-active enzymes (for example glycoside hydrolases). The majority of these domains have carbohydrate-binding activity. Some of these domains are found on cellulosomal scaffoldin proteins. CBMs were previously known as cellulose-binding domains.[1] CBMs are classified into numerous families, based on amino acid sequence similarity. There are currently (June 2011) 64 families of CBM in the CAZy database.[2]

CBMs of microbial glycoside hydrolases play a central role in the recycling of photosynthetically fixed carbon through their binding to specific plant structural polysaccharides.[3] CBMs can recognise both crystalline and amorphous cellulose forms.[4] CBMs are the most common non-catalytic modules associated with enzymes active in plant cell-wall hydrolysis. Many putative CBMs have been identified by amino acid sequence alignments but only a few representatives have been shown experimentally to have a carbohydrate-binding function.[5]

CBM1

[edit]

Carbohydrate-binding module family 1 (CBM1) consists of 36 amino acids. This domain contains 4 conserved cysteine residues which are involved in the formation of two disulfide bonds.

CBM2

[edit]

Carbohydrate-binding module family 2 (CBM2) contains two conserved cysteines - one at each extremity of the domain - which have been shown [6] to be involved in a disulfide bond. There are also four conserved tryptophans, two of which are involved in cellulose binding.[7][8][9]

CBM3

[edit]

Carbohydrate-binding module family 3 (CBM3) is involved in cellulose binding [10] and is found associated with a wide range of bacterial glycosyl hydrolases. The structure of this domain is known; it forms a beta sandwich.[11]

CBM4

[edit]

Carbohydrate-binding module family 4 (CBM4) includes the two cellulose-binding domains, CBD(N1) and CBD(N2), arranged in tandem at the N terminus of the 1,4-beta-glucanase, CenC, from Cellulomonas fimi. These homologous CBMs are distinct in their selectivity for binding amorphous and not crystalline cellulose.[12] Multidimensional heteronuclear nuclear magnetic resonance (NMR) spectroscopy was used to determine the tertiary structure of the 152 amino acid N-terminal cellulose-binding domain from C. fimi 1,4-beta-glucanase CenC (CBDN1). The tertiary structure of CBDN1 is strikingly similar to that of the bacterial 1,3-1,4-beta-glucanases, as well as other sugar-binding proteins with jelly-roll folds.[13] CBM4 and CBM9 are closely related.

CBM5

[edit]

Carbohydrate-binding module family 5 (CBM5) binds chitin.[14] CBM5 and CBM12 are distantly related.

CBM6

[edit]

Carbohydrate-binding module family 6 (CBM6) is unusual in that it contains two substrate-binding sites, cleft A and cleft B. Cellvibrio mixtus endoglucanase 5A contains two CBM6 domains, the CBM6 domain at the C-terminus displays distinct ligand binding specificities in each of the substrate-binding clefts. Both cleft A and cleft B can bind cello-oligosaccharides, laminarin preferentially binds in cleft A, xylooligosaccharides only bind in cleft A and beta1,4,-beta1,3-mixed linked glucans only bind in cleft B.[15]

CBM9

[edit]

Carbohydrate-binding module family 9 (CBM9) binds to crystalline cellulose.[16] CBM4 and CBM9 are closely related.

CBM10

[edit]

Carbohydrate-binding module family 10 (CBM10) is found in two distinct sets of proteins with different functions. Those found in aerobic bacteria bind cellulose (or other carbohydrates); but in anaerobic fungi they are protein binding domains, referred to as dockerin domains. The dockerin domains are believed to be responsible for the assembly of a multiprotein cellulase/hemicellulase complex, similar to the cellulosome found in certain anaerobic bacteria.[17][18]

In anaerobic bacteria that degrade plant cell walls, exemplified by Clostridium thermocellum, the dockerin domains of the catalytic polypeptides can bind equally well to any cohesin from the same organism. More recently, anaerobic fungi, typified by Piromyces equi, have been suggested to also synthesise a cellulosome complex, although the dockerin sequences of the bacterial and fungal enzymes are completely different.[19] For example, the fungal enzymes contain one, two or three copies of the dockerin sequence in tandem within the catalytic polypeptide. In contrast, all the C. thermocellum cellulosome catalytic components contain a single dockerin domain. The anaerobic bacterial dockerins are homologous to EF hands (calcium-binding motifs) and require calcium for activity whereas the fungal dockerin does not require calcium. Finally, the interaction between cohesin and dockerin appears to be species specific in bacteria, there is almost no species specificity of binding within fungal species and no identified sites that distinguish different species.

The of dockerin from P. equi contains two helical stretches and four short beta-strands which form an antiparallel sheet structure adjacent to an additional short twisted parallel strand. The N- and C-termini are adjacent to each other.[19]

CBM11

[edit]

Carbohydrate-binding module family 11 (CBM11) is found in a number of bacterial cellulases. One example is the CBM11 of Clostridium thermocellum Cel26A-Cel5E, this domain has been shown to bind both β-1,4-glucan and β-1,3-1,4-mixed linked glucans.[20] CBM11 has beta-sandwich structure with a concave side forming a substrate-binding cleft.[20]

CBM12

[edit]

Carbohydrate-binding module family 12 (CBM12) comprises two beta-sheets, consisting of two and three antiparallel beta strands respectively. It binds chitin via the aromatic rings of tryptophan residues.[14] CBM5 and CBM12 are distantly related.

CBM14

[edit]

Carbohydrate-binding module family 14 (CBM14) is also known as the peritrophin-A domain. It is found in chitin binding proteins, particularly the peritrophic matrix proteins of insects and animal chitinases.[21][22][23] Copies of the domain are also found in some baculoviruses. It is an extracellular domain that contains six conserved cysteines that probably form three disulfide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.[21]

CBM15

[edit]

Carbohydrate-binding module family 15 (CBM15), found in bacterial enzymes, has been shown to bind to xylan and xylooligosaccharides. It has a beta-jelly roll fold, with a groove on the concave surface of one of the beta-sheets.[3]

CBM17

[edit]

Carbohydrate-binding module family 17 (CBM17) appears to have a very shallow binding cleft that may be more accessible to cellulose chains in non-crystalline cellulose than the deeper binding clefts of family 4 CBMs.[24] Sequence and structural conservation in families CBM17 and CBM28 suggests that they have evolved through gene duplication and subsequent divergence.[4] CBM17 does not compete with CBM28 modules when binding to non-crystalline cellulose. Different CBMs have been shown to bind to different sites in amorphous cellulose, CBM17 and CBM28 recognise distinct non-overlapping sites in amorphous cellulose.[25]

CBM18

[edit]

Carbohydrate-binding module family 18 (CBM18) (also known as chitin binding 1 or chitin recognition protein) is found in a number of plant and fungal proteins that bind N-acetylglucosamine (e.g. solanaceous lectins of tomato and potato, plant endochitinases, the wound-induced proteins: hevein, win1 and win2, and the Kluyveromyces lactis killer toxin alpha subunit).[26] The domain may occur in one or more copies and is thought to be involved in recognition or binding of chitin subunits.[27][28] In chitinases, as well as in the potato wound-induced proteins, this 43-residue domain directly follows the signal sequence and is therefore at the N terminus of the mature protein; in the killer toxin alpha subunit it is located in the central section of the protein.

CBM19

[edit]

Carbohydrate-binding module family 19 (CBM19), found in fungal chitinases, binds chitin.[29]

CBM20

[edit]

Carbohydrate-binding module family 20 (CBM20) binds to starch.[30][31]

CBM21

[edit]

Carbohydrate-binding module family 21 (CBM21), found in many eukaryotic proteins involved in glycogen metabolism, binds to glycogen.[32]

CBM25

[edit]

Carbohydrate-binding module family 25 (CBM25) binds alpha-glucooligosaccharides, particularly those containing alpha-1,6 linkages, and granular starch.[33]

CBM27

[edit]

Carbohydrate-binding module family 27 (CBM27) binds to beta-1,4-mannooligosaccharides, carob galactomannan, and konjac glucomannan, but not to cellulose (insoluble and soluble) or soluble birchwood xylan. CBM27 adopts a beta sandwich structure comprising 13 beta strands with a single, small alpha-helix and a single metal atom.[34]

CBM28

[edit]

Carbohydrate-binding module family 28 (CBM28) does not compete with CBM17 modules when binding to non-crystalline cellulose. Different CBMs have been shown to bind to different sirtes in amorphous cellulose, CBM17 and CBM28 recognise distinct non-overlapping sites in amorphous cellulose. CBM28 has a "beta-jelly roll" topology, which is similar in structure to the CBM17 domains. Sequence and structural conservation in families CBM17 and CBM28 suggests that they have evolved through gene duplication and subsequent divergence.[4][25]

CBM32

[edit]

Carbohydrate-binding module family 32 (CBM32) binds to diverse substrates, ranging from plant cell wall polysaccharides to complex glycans.[35] The module has so far been found in microorganisms, including archea, eubacteria and fungi.[35] CBM32 adopts a beta-sandwich fold and has a bound metal atom, most often observed to be calcium.[36] CBM32 modules are associated with catalytic modules such as sialidases, B-N-acetylglucosaminidases, α-N-acetylglucosaminidases, mannanases and galactose oxidases.[36]

CBM33

[edit]

Carbohydrate-binding module family 33 (CBM33) is a chitin-binding domain.[37] It has a budded fibronectin type III fold consisting of two beta-sheets, arranged as a beta-sheet sandwich and a bud consisting of three short helices, located between beta-strands 1 and 2. It binds chitin via conserved polar amino acids.[38] This domain is found in isolation in baculoviral spheroidin and spindolin proteins.

CBM48

[edit]

Carbohydrate-binding module family 48 (CBM48) is often found in enzymes containing glycosyl hydrolase family 13 catalytic domains. It is found in a range of enzymes that act on branched substrates i.e. isoamylase, pullulanase and branching enzyme. Isoamylase hydrolyses 1,6-alpha-D-glucosidic branch linkages in glycogen, amylopectin and dextrin; 1,4-alpha-glucan branching enzyme functions in the formation of 1,6-glucosidic linkages of glycogen; and pullulanase is a starch-debranching enzyme. CBM48 binds glycogen.[39][40][41][42]

CBM49

[edit]

Carbohydrate-binding module family 49 (CBM49) is found at the C-terminal of cellulases and in vitro binding studies have shown it to binds to crystalline cellulose.[43]

References

[edit]
  1. ^ Gilkes NR, Henrissat B, Kilburn DG, Miller RC, Warren RA (June 1991). "Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families". Microbiol. Rev. 55 (2): 303–15. doi:10.1128/MMBR.55.2.303-315.1991. PMC 372816. PMID 1886523.
  2. ^ Cantarel, B. L.; Coutinho, P. M.; Rancurel, C.; Bernard, T.; Lombard, V.; Henrissat, B. (2009). "The Carbohydrate-Active EnZymes database (CAZy): An expert resource for Glycogenomics". Nucleic Acids Research. 37 (Database issue): D233–D238. doi:10.1093/nar/gkn663. PMC 2686590. PMID 18838391.
  3. ^ a b Szabo, L.; Jamal, S.; Xie, H.; Charnock, S. J.; Bolam, D. N.; Gilbert, H. J.; Davies, G. J. (2001). "Structure of a Family 15 Carbohydrate-binding Module in Complex with Xylopentaose. Evidence that xylan binds in an approximate 3-fold helical conformation". Journal of Biological Chemistry. 276 (52): 49061–49065. doi:10.1074/jbc.M109558200. PMID 11598143.
  4. ^ a b c Jamal S, Nurizzo D, Boraston AB, Davies GJ (May 2004). "X-ray crystal structure of a non-crystalline cellulose-specific carbohydrate-binding module: CBM28". J. Mol. Biol. 339 (2): 253–8. doi:10.1016/j.jmb.2004.03.069. PMID 15136030.
  5. ^ Roske Y, Sunna A, Pfeil W, Heinemann U (July 2004). "High-resolution crystal structures of Caldicellulosiruptor strain Rt8B.4 carbohydrate-binding module CBM27-1 and its complex with mannohexaose". J. Mol. Biol. 340 (3): 543–54. doi:10.1016/j.jmb.2004.04.072. PMID 15210353.
  6. ^ Gilkes NR, Claeyssens M, Aebersold R, Henrissat B, Meinke A, Morrison HD, Kilburn DG, Warren RA, Miller RC (December 1991). "Structural and functional relationships in two families of beta-1,4-glycanases". Eur. J. Biochem. 202 (2): 367–77. doi:10.1111/j.1432-1033.1991.tb16384.x. PMID 1761039.
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  12. ^ Brun E, Johnson PE, Creagh AL, Tomme P, Webster P, Haynes CA, McIntosh LP (March 2000). "Structure and binding specificity of the second N-terminal cellulose-binding domain from Cellulomonas fimi endoglucanase C". Biochemistry. 39 (10): 2445–58. doi:10.1021/bi992079u. PMID 10704194.
  13. ^ Johnson PE, Joshi MD, Tomme P, Kilburn DG, McIntosh LP (November 1996). "Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy". Biochemistry. 35 (45): 14381–94. doi:10.1021/bi961612s. PMID 8916925.
  14. ^ a b Akagi, K. -I.; Watanabe, J.; Hara, M.; Kezuka, Y.; Chikaishi, E.; Yamaguchi, T.; Akutsu, H.; Nonaka, T.; Watanabe, T.; Ikegami, T. (2006). "Identification of the Substrate Interaction Region of the Chitin-Binding Domain of Streptomyces griseus Chitinase C". Journal of Biochemistry. 139 (3): 483–493. doi:10.1093/jb/mvj062. PMID 16567413.
  15. ^ Henshaw, J. L.; Bolam, D. N.; Pires, V. M.; Czjzek, M.; Henrissat, B.; Ferreira, L. M.; Fontes, C. M.; Gilbert, H. J. (2004). "The Family 6 Carbohydrate Binding Module CmCBM6-2 Contains Two Ligand-binding Sites with Distinct Specificities". Journal of Biological Chemistry. 279 (20): 21552–21559. doi:10.1074/jbc.M401620200. PMID 15004011.
  16. ^ Winterhalter, C.; Heinrich, P.; Candussio, A.; Wich, G.; Liebl, W. (1995). "Identification of a novel cellulose-binding domain within the multidomain 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima". Molecular Microbiology. 15 (3): 431–444. doi:10.1111/j.1365-2958.1995.tb02257.x. PMID 7783614. S2CID 25985173.
  17. ^ Millward-Sadler SJ, Davidson K, Hazlewood GP, Black GW, Gilbert HJ, Clarke JH (November 1995). "Novel cellulose-binding domains, NodB homologues and conserved modular architecture in xylanases from the aerobic soil bacteria Pseudomonas fluorescens subsp. cellulosa and Cellvibrio mixtus". Biochem. J. 312 (1): 39–48. doi:10.1042/bj3120039. PMC 1136224. PMID 7492333.
  18. ^ Fanutti C, Ponyi T, Black GW, Hazlewood GP, Gilbert HJ (December 1995). "The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain". J. Biol. Chem. 270 (49): 29314–22. doi:10.1074/jbc.270.49.29314. PMID 7493964.
  19. ^ a b Raghothama S, Eberhardt RY, Simpson P, Wigelsworth D, White P, Hazlewood GP, Nagy T, Gilbert HJ, Williamson MP (September 2001). "Characterization of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi". Nat. Struct. Biol. 8 (9): 775–8. doi:10.1038/nsb0901-775. PMID 11524680. S2CID 6442375.
  20. ^ a b Carvalho, A. L.; Goyal, A.; Prates, J. A.; Bolam, D. N.; Gilbert, H. J.; Pires, V. M.; Ferreira, L. M.; Planas, A.; Romão, M. J.; Fontes, C. M. (2004). "The Family 11 Carbohydrate-binding Module of Clostridium thermocellum Lic26A-Cel5E Accommodates -1,4- and -1,3-1,4-Mixed Linked Glucans at a Single Binding Site". Journal of Biological Chemistry. 279 (33): 34785–34793. doi:10.1074/jbc.M405867200. PMID 15192099.
  21. ^ a b Shen Z, Jacobs-Lorena M (July 1998). "A type I peritrophic matrix protein from the malaria vector Anopheles gambiae binds to chitin. Cloning, expression, and characterization". J. Biol. Chem. 273 (28): 17665–70. doi:10.1074/jbc.273.28.17665. PMID 9651363.
  22. ^ Elvin CM, Vuocolo T, Pearson RD, East IJ, Riding GA, Eisemann CH, Tellam RL (April 1996). "Characterization of a major peritrophic membrane protein, peritrophin-44, from the larvae of Lucilia cuprina. cDNA and deduced amino acid sequences". J. Biol. Chem. 271 (15): 8925–35. doi:10.1074/jbc.271.15.8925. PMID 8621536.
  23. ^ Casu R, Eisemann C, Pearson R, Riding G, East I, Donaldson A, Cadogan L, Tellam R (August 1997). "Antibody-mediated inhibition of the growth of larvae from an insect causing cutaneous myiasis in a mammalian host". Proc. Natl. Acad. Sci. U.S.A. 94 (17): 8939–44. Bibcode:1997PNAS...94.8939C. doi:10.1073/pnas.94.17.8939. PMC 22971. PMID 9256413.
  24. ^ Notenboom V, Boraston AB, Chiu P, Freelove AC, Kilburn DG, Rose DR (December 2001). "Recognition of cello-oligosaccharides by a family 17 carbohydrate-binding module: an X-ray crystallographic, thermodynamic and mutagenic study". J. Mol. Biol. 314 (4): 797–806. doi:10.1006/jmbi.2001.5153. PMID 11733998.
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