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Nature Structural Biology  6, 990 - 991 (1999)
doi:10.1038/14870

A chaperone with a hydrophilic surface

Nicholas J. Cowan & Sally A. Lewis

Nicholas J. Cowan and Sally A. Lewis are in the Department of Biochemistry, New York University Medical Center, 550 First Avenue, New York, New York 10016, USA.

Correspondence should be addressed to Nicholas J. Cowan cowann01@mcrcr.med.nyu.edu.
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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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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