A chaperone with a hydrophilic surface. |
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| Authors: | N J Cowan S A Lewis |
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| Affiliation: | Department of Biochemistry, New York University Medical Center, 550 First Avenue, New York, New York 10016, USA. cowann01@mcrcr.med.nyu.edu |
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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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