From Wikipedia, the free encyclopedia
Jump to: navigation, search
Crystallin, gamma B
PDB 2jdf EBI.png
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols CRYGB ; CRYG2; CTRCT39
External IDs OMIM123670 MGI88522 HomoloGene3816 GeneCards: CRYGB Gene
RNA expression pattern
PBB GE CRYGB 207715 at tn.png
More reference expression data
Species Human Mouse
Entrez 1419 12965
Ensembl ENSG00000182187 ENSMUSG00000073658
UniProt P07316 P04344
RefSeq (mRNA) NM_005210 NM_144761
RefSeq (protein) NP_005201 NP_658906
Location (UCSC) Chr 2:
209.01 – 209.01 Mb
Chr 1:
65.08 – 65.08 Mb
PubMed search [1] [2]

Gamma-crystallin B is a protein that in humans is encoded by the CRYGB gene.[1]

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- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.[1]


Further reading[edit]