1bd7

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{{STRUCTURE_1bd7| PDB=1bd7 | SCENE= }}
{{STRUCTURE_1bd7| PDB=1bd7 | SCENE= }}
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'''CIRCULARLY PERMUTED BB2-CRYSTALLIN'''
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===CIRCULARLY PERMUTED BB2-CRYSTALLIN===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9655330 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9655330}}
==About this Structure==
==About this Structure==
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[[Category: Eye-lens protein]]
[[Category: Eye-lens protein]]
[[Category: Multigene family]]
[[Category: Multigene family]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:21:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:52:34 2008''

Revision as of 15:52, 30 June 2008

Image:1bd7.png

Template:STRUCTURE 1bd7

CIRCULARLY PERMUTED BB2-CRYSTALLIN

Template:ABSTRACT PUBMED 9655330

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

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