File:Interface on the N-SH2 binding site and FGFR1 kinase.jpg
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Summary
| Description |
English: The FGFR1 kinase is bound to the N-SH2 domain primarily through charged amino acids. Arginine residue (R609) on the N-SH2 domain forms a salt bridge to aspartate 755 (D755) on the FGFR1 domain. The acid base pair located in the middle of the interface are nearly parallel to each other, indicating a highly favorable interaction. N-SH2 domain makes an additional polar contact through water-mediated interaction that takes place between the N-SH2 domain and FGFR1 kinase. Interestingly, the arginine residue 609 (R609) on the FGFR1 kinase also forms a salt bridge to the aspartate residue (D594) on the N-SH2 domain. The acid-base pair interacts with each other carry out redox reaction to stabilize the complex. |
| Date | |
| Source | Own work |
| Author | ChinHT |
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 03:27, 18 April 2016 | | 860 × 652 (231 KB) | ChinHT | User created page with UploadWizard |
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