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2QLD

human Hsp40 Hdj1

Summary for 2QLD
Entry DOI10.2210/pdb2qld/pdb
DescriptorDnaJ homolog subfamily B member 1 (1 entity in total)
Functional Keywordsprimarily beta sheets, chaperone
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: P25685
Total number of polymer chains1
Total formula weight20737.21
Authors
Hu, J.,Wu, Y.,Li, J.,Fu, Z.,Sha, B. (deposition date: 2007-07-12, release date: 2008-07-15, Last modification date: 2024-04-03)
Primary citationHu, J.,Wu, Y.,Li, J.,Qian, X.,Fu, Z.,Sha, B.
The crystal structure of the putative peptide-binding fragment from the human Hsp40 protein Hdj1.
Bmc Struct.Biol., 8:3-3, 2008
Cited by
PubMed Abstract: The mechanism by which Hsp40 and other molecular chaperones recognize and interact with non-native polypeptides is a fundamental question. How Hsp40 co-operates with Hsp70 to facilitate protein folding is not well understood. To investigate the mechanisms, we determined the crystal structure of the putative peptide-binding fragment of Hdj1, a human member of the type II Hsp40 family.
PubMed: 18211704
DOI: 10.1186/1472-6807-8-3
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

239149

건을2025-07-23부터공개중

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