3IAW
Crystal structure of a chemically synthesized 203 amino acid 'covalent dimer' [Gly51;Aib51']HIV-1 protease molecule complexed with MVT-101 reduced isostere inhibitor at 1.6 A resolution
Summary for 3IAW
| Entry DOI | 10.2210/pdb3iaw/pdb |
| Related | 3FSM 3HAU 3HAW 3HBO 3HDK 3HLO |
| Related PRD ID | PRD_000398 |
| Descriptor | [Gly51;Aib51'] 'covalent dimer' HIV-1 protease, N-{(2S)-2-[(N-acetyl-L-threonyl-L-isoleucyl)amino]hexyl}-L-norleucyl-L-glutaminyl-N~5~-[amino(iminio)methyl]-L-ornithinamide, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | asymmetric dimer, covalent dimer, beta-sheet, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Total number of polymer chains | 1 |
| Total formula weight | 22786.75 |
| Authors | Torbeev, V.Y.,Kent, S.B.H. (deposition date: 2009-07-14, release date: 2011-04-27, Last modification date: 2012-12-12) |
| Primary citation | Torbeev, V.Y.,Raghuraman, H.,Hamelberg, D.,Tonelli, M.,Westler, W.M.,Perozo, E.,Kent, S.B. Protein conformational dynamics in the mechanism of HIV-1 protease catalysis. Proc.Natl.Acad.Sci.USA, 108:20982-20987, 2011 Cited by PubMed Abstract: We have used chemical protein synthesis and advanced physical methods to probe dynamics-function correlations for the HIV-1 protease, an enzyme that has received considerable attention as a target for the treatment of AIDS. Chemical synthesis was used to prepare a series of unique analogues of the HIV-1 protease in which the flexibility of the "flap" structures (residues 37-61 in each monomer of the homodimeric protein molecule) was systematically varied. These analogue enzymes were further studied by X-ray crystallography, NMR relaxation, and pulse-EPR methods, in conjunction with molecular dynamics simulations. We show that conformational isomerization in the flaps is correlated with structural reorganization of residues in the active site, and that it is preorganization of the active site that is a rate-limiting factor in catalysis. PubMed: 22158985DOI: 10.1073/pnas.1111202108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.61 Å) |
Structure validation
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