1bd7: Difference between revisions
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{{STRUCTURE_1bd7| PDB=1bd7 | SCENE= }} | |||
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'''CIRCULARLY PERMUTED BB2-CRYSTALLIN''' | '''CIRCULARLY PERMUTED BB2-CRYSTALLIN''' | ||
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[[Category: Slingsby, C.]] | [[Category: Slingsby, C.]] | ||
[[Category: Wright, G.]] | [[Category: Wright, G.]] | ||
[[Category: | [[Category: Beta-crystallin b]] | ||
[[Category: | [[Category: Eye-lens protein]] | ||
[[Category: | [[Category: Multigene family]] | ||
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Revision as of 08:21, 2 May 2008
CIRCULARLY PERMUTED BB2-CRYSTALLIN
Overview
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.
About this Structure
1BD7 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 11:21:44 2008
