Structural highlights
Function
[CRBB2_RAT] Crystallins are the dominant structural components of the vertebrate eye lens.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The betagamma-crystallins form a superfamily of eye lens proteins comprised of multiple Greek motifs that are symmetrically organized into domains and higher assemblies. In the betaB2-crystallin dimer each polypeptide folds into two similar domains that are related to monomeric gamma-crystallin by domain swapping. The crystal structure of the circularly permuted two-domain betaB2 polypeptide shows that permutation converts intermolecular domain pairing into intramolecular pairing. However, the dimeric permuted protein is, in fact, half a native tetramer. This result shows how the sequential order of domains in multi-domain proteins can affect quaternary domain assembly.
Circular permutation of betaB2-crystallin changes the hierarchy of domain assembly.,Wright G, Basak AK, Wieligmann K, Mayr EM, Slingsby C Protein Sci. 1998 Jun;7(6):1280-5. PMID:9655330[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wright G, Basak AK, Wieligmann K, Mayr EM, Slingsby C. Circular permutation of betaB2-crystallin changes the hierarchy of domain assembly. Protein Sci. 1998 Jun;7(6):1280-5. PMID:9655330
