A chaperone with a hydrophilic surface.

N J Cowan; S A Lewis

doi:10.1038/14870

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PubMed · 10542082

A chaperone with a hydrophilic surface.

N J Cowan·S A Lewis

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Abstract

The folding of native tubulin involves at least seven different chaperone proteins: prefoldin, the cytosolic chaperonin CCT and five tubulin-specific chaperone proteins named cofactors A-E. The structure of the yeast homolog of cofactor A, Rbl2p, shows it to be a dimer with largely hydrophilic surfaces, reflecting the fact that it interacts with quasi-native, not unfolded, beta-tubulin.

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Animals Microtubule-Associated Proteins Models, Biological Molecular Chaperones Protein Binding Protein Folding Protein Structure, Quaternary Saccharomyces cerevisiae Proteins Static Electricity Tubulin Comment News

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N J Cowan, S A Lewis. 1999. A chaperone with a hydrophilic surface.. https://doi.org/10.1038/14870

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