Hsp40: Difference between revisions
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=='Hsp40s'== | =='Hsp40s'== | ||
<StructureSection load='2QLD' size='340' side='right' caption='Human Hsp40 Hdj1' scene=''> | <StructureSection load='2QLD' size='340' side='right' caption='Human Hsp40 Hdj1 (PDB code [[2qld]]).' scene=''> | ||
These proteins ( J protein) and NEF cochaperones regulate the Hsp70 reaction cycle. The Hsp40 proteins constitute a large family with more than 40 members in | These proteins ( J protein) and NEF cochaperones regulate the Hsp70 reaction cycle. The Hsp40 proteins constitute a large family with more than 40 members in | ||
Latest revision as of 11:59, 28 December 2014
'Hsp40s'
<StructureSection load='2QLD' size='340' side='right' caption='Human Hsp40 Hdj1 (PDB code 2qld).' scene=>
These proteins ( J protein) and NEF cochaperones regulate the Hsp70 reaction cycle. The Hsp40 proteins constitute a large family with more than 40 members in humans. All of them contain a J domain, which binds to the N-terminal ATPase domain of Hsp70 and the adjacent linker region. Canonical Hsp40s (members of classes I and II) function as chaperones independently and recruit Hsp70 to nonnative substrate proteins. Other Hsp40s (class III) are more diverse and combine the J domain with a variety of functional modules. The interaction with Hsp70 strongly stimulates the hydrolysis of Hsp70-bound ATP to ADP, resulting in stable substrate binding by Hsp70 in the closed conformation [1] to the rescue.
References
- ↑ Kim YE, Hipp MS, Bracher A, Hayer-Hartl M, Hartl FU. Molecular chaperone functions in protein folding and proteostasis. Annu Rev Biochem. 2013;82:323-55. doi: 10.1146/annurev-biochem-060208-092442. PMID:23746257 doi:https://dx.doi.org/10.1146/annurev-biochem-060208-092442
