Structural highlights
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
