1bd7 | pdb_00001bd7

CIRCULARLY PERMUTED BB2-CRYSTALLIN

spinqualitylabelsall models 1bd7, resolution 2.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1bd7 is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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