3K60
Crystal structure of N-terminal domain of Plasmodium falciparum Hsp90 (PF07_0029) bound to ADP
Summary for 3K60
| Entry DOI | 10.2210/pdb3k60/pdb |
| Related | 1Y6Z 3IED |
| Descriptor | Heat shock protein 86, ADENOSINE-5'-DIPHOSPHATE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | chaperone, atpase, stress response |
| Biological source | Plasmodium falciparum More |
| Total number of polymer chains | 2 |
| Total formula weight | 51480.37 |
| Authors | Corbett, K.D.,Berger, J.M. (deposition date: 2009-10-08, release date: 2010-08-18, Last modification date: 2023-09-06) |
| Primary citation | Corbett, K.D.,Berger, J.M. Structure of the ATP-binding domain of Plasmodium falciparum Hsp90. Proteins, 78:2738-2744, 2010 Cited by PubMed Abstract: Hsp90 is an important cellular chaperone and attractive target for therapeutics against both cancer and infectious organisms. The Hsp90 protein from the parasite Plasmodium falciparum, the causative agent of malaria, is critical for this organism's survival; the anti-Hsp90 drug geldanamycin is toxic to P. falciparum growth. We have solved the structure of the N-terminal ATP-binding domain of P. falciparum Hsp90, which contains a principal drug-binding pocket, in both apo and ADP-bound states at 2.3 A resolution. The structure shows that P. falciparum Hsp90 is highly similar to human Hsp90, and likely binds agents such as geldanamycin in an identical manner. Our results should aid in the structural understanding of Hsp90-drug interactions in P. falciparum, and provide a scaffold for future drug-discovery efforts. PubMed: 20635416DOI: 10.1002/prot.22799 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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