期刊
PROTEIN AND PEPTIDE LETTERS
卷 16, 期 6, 页码 606-612出版社
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/092986609788490159
关键词
Molecular chaperone; Hsp40; Hsp70; J-domain; peptide-binding fragment; protein structure; Sis1; Ydj1
资金
- NIDDK NIH HHS [R01 DK056203-10, R01 DK056203] Funding Source: Medline
- NIGMS NIH HHS [R01 GM080261-03, R01 GM080261] Funding Source: Medline
The mechanism by which Hsp40 and other molecular chaperones recognize and interact with non-native polypeptides is a fundamental question, as is how Hsp40 co-operates with Hsp70 to facilitate protein folding. Years of structural studies of Hsp40 from yeast and other species, conducted using X-ray protein crystallography, NMR and small-angle X-ray scattering, have shed light on the mechanisms how Hsp40 functions as a molecular chaperone and how Hsp40-Hsp70 pair promotes protein folding, protein transport and degradation. This review provides a discussion of recent structural studies of Hsp40s and their functional implications.
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