2PSV
Crystal Structure of wild type HIV-1 protease in complex with CARB-KB45
Summary for 2PSV
| Entry DOI | 10.2210/pdb2psv/pdb |
| Related | 2psu |
| Descriptor | Protease, PHOSPHATE ION, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | drug design, hiv-1 protease, protease inhibitors, hydrolase |
| Biological source | Human immunodeficiency virus 1 |
| Total number of polymer chains | 2 |
| Total formula weight | 22453.11 |
| Authors | Schiffer, C.A.,Nalam, M.N.L. (deposition date: 2007-05-07, release date: 2007-06-05, Last modification date: 2023-08-30) |
| Primary citation | Chellappan, S.,Kiran Kumar Reddy, G.S.,Ali, A.,Nalam, M.N.,Anjum, S.G.,Cao, H.,Kairys, V.,Fernandes, M.X.,Altman, M.D.,Tidor, B.,Rana, T.M.,Schiffer, C.A.,Gilson, M.K. Design of Mutation-resistant HIV Protease Inhibitors with the Substrate Envelope Hypothesis. Chem.Biol.Drug Des., 69:298-313, 2007 Cited by PubMed Abstract: There is a clinical need for HIV protease inhibitors that can evade resistance mutations. One possible approach to designing such inhibitors relies upon the crystallographic observation that the substrates of HIV protease occupy a rather constant region within the binding site. In particular, it has been hypothesized that inhibitors which lie within this region will tend to resist clinically relevant mutations. The present study offers the first prospective evaluation of this hypothesis, via computational design of inhibitors predicted to conform to the substrate envelope, followed by synthesis and evaluation against wild-type and mutant proteases, as well as structural studies of complexes of the designed inhibitors with HIV protease. The results support the utility of the substrate envelope hypothesis as a guide to the design of robust protease inhibitors. PubMed: 17539822DOI: 10.1111/j.1747-0285.2007.00514.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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