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, β-tubulin.
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Cowan, N., Lewis, S. A chaperone with a hydrophilic surface. Nat Struct Mol Biol 6, 990–991 (1999). https://doi.org/10.1038/14870
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DOI: https://doi.org/10.1038/14870
