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Article

Mutation of interfaces in domain-swapped human betaB2-crystallin.

Protein science : a publication of the Protein Society - 1 Apr 2007

Smith Myron A, Bateman Orval A, Jaenicke Rainer, Slingsby Christine

Abstract excerpt

The superfamily of eye lens betagamma-crystallins is highly modularized, with Greek key motifs being used to form symmetric domains. Sequences of monomeric gamma-crystallins and oligomeric beta-crystallins fold into two domains that pair about a further conserved symmetric interface. Conservation of this assembly interface by domain swapping is the device adopted by family member betaB2-crystallin to form a...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 17327390
DOI: 10.1110/ps.062659107
PMCID: PMC2203347

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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