Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N-terminal and C-terminal extensions. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta basic group member, is part of a gene cluster with beta-A4, beta-B1, and beta-B3. A chain-terminating mutation was found to cause type 2 cerulean cataracts.[7]
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Aarts HJ, Den Dunnen JT, Lubsen NH, Schoenmakers JG (1988). "Linkage between the beta B2 and beta B3 crystallin genes in man and rat: a remnant of an ancient beta-crystallin gene cluster". Gene. 59 (1): 127–35. doi:10.1016/0378-1119(87)90273-3. PMID3436525.
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Hanson SR, Hasan A, Smith DL, Smith JB (2000). "The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage". Exp. Eye Res. 71 (2): 195–207. doi:10.1006/exer.2000.0868. PMID10930324.
