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. 1998 Jun;7(6):1280–1285. doi: 10.1002/pro.5560070602

Circular permutation of betaB2-crystallin changes the hierarchy of domain assembly.

G Wright 1, A K Basak 1, K Wieligmann 1, E M Mayr 1, C Slingsby 1
PMCID: PMC2144035  PMID: 9655330

Abstract

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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Selected References

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