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• W2132103632 endingPage "625" @default.
• W2132103632 startingPage "615" @default.
• W2132103632 abstract "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 solution dimer. However, the betaB1-crystallin solution dimer is formed from an interface used by the domain-swapped dimer to form a tetramer in the crystal lattice. Comparison of these two structures indicated an intriguing relationship between linker conformation, interface ion pair networks, and higher assembly. Here the X-ray structure of recombinant human betaB2-crystallin showed that domain swapping was determined by the sequence and not assembly conditions. The solution characteristics of mutants that were designed to alter an ion pair network at a higher assembly interface and a mutant that changed a proline showed they remained dimeric. X-ray crystallography showed that the dimeric mutants did not reverse domain swapping. Thus, the sequence of betaB2-crystallin appears well optimized for domain swapping. However, a charge-reversal mutation to the conserved domain-pairing interface showed drastic changes to solution behavior. It appears that the higher assembly of the betagamma-crystallin domains has exploited symmetry to create diversity while avoiding aggregation. These are desirable attributes for proteins that have to exist at very high concentration for a very long time." @default.
• W2132103632 created "2016-06-24" @default.
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• W2132103632 creator A5023088787 @default.
• W2132103632 creator A5031189482 @default.
• W2132103632 date "2007-04-01" @default.
• W2132103632 modified "2023-10-09" @default.
• W2132103632 title "Mutation of interfaces in domain-swapped human betaB2-crystallin" @default.
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• W2132103632 doi "https://doi.org/10.1110/ps.062659107" @default.
• W2132103632 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2203347" @default.
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• W2132103632 hasPublicationYear "2007" @default.
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