2QLD
human Hsp40 Hdj1
Summary for 2QLD
Entry DOI | 10.2210/pdb2qld/pdb |
Descriptor | DnaJ homolog subfamily B member 1 (1 entity in total) |
Functional Keywords | primarily beta sheets, chaperone |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm: P25685 |
Total number of polymer chains | 1 |
Total formula weight | 20737.21 |
Authors | |
Primary citation | Hu, 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: 18211704DOI: 10.1186/1472-6807-8-3 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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