Other
1 Publications
First Author | Title | Year | Journal | Volume | Pages |
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Zhu X | Structural analysis of substrate binding by the molecular chaperone DnaK. | 1996 | Science | 272 | 1606-14 |
Name | Heat shock protein 70kD, C-terminal domain | Short Name | HSP70_C |
Type | Domain | Description | Members of the 70-kilodalton heat-shock protein (HSP70) family promote protein folding both constitutively and in response to stress. These proteins have two functional units: a substrate-binding unit, and an adenosine triphosphatase unit. The substrate-binding unit of DnaK consists of a beta-sandwich domain followed by alpha-helical segments. The alpha-helical domain stabilises the complex, but does not contact the peptide directly [].This entry represents the C-terminal alpha-helical subdomain of the substrate-binding unit from DnaK and other HSP70 proteins. |
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First Author | Title | Year | Journal | Volume | Pages |
---|---|---|---|---|---|
Zhu X | Structural analysis of substrate binding by the molecular chaperone DnaK. | 1996 | Science | 272 | 1606-14 |
To cite PlanMine, please refer to the following publication:Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C. |