1LV1
Crystal Structure Analysis of the non-active site mutant of tethered HIV-1 protease to 2.1A resolution
Summary for 1LV1
| Entry DOI | 10.2210/pdb1lv1/pdb |
| Related | 1G6L |
| Descriptor | HIV-1 protease (2 entities in total) |
| Functional Keywords | beta-ribbon flap, hydrolase |
| Biological source | Human immunodeficiency virus 1 More |
| Cellular location | Gag-Pol polyprotein: Host cell membrane; Lipid-anchor . Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P04585 |
| Total number of polymer chains | 1 |
| Total formula weight | 21902.76 |
| Authors | Kumar, M.,Kannan, K.K.,Hosur, M.V.,Bhavesh, N.S.,Chatterjee, A.,Mittal, R.,Hosur, R.V. (deposition date: 2002-05-24, release date: 2002-06-19, Last modification date: 2024-05-29) |
| Primary citation | Kumar, M.,Kannan, K.K.,Hosur, M.V.,Bhavesh, N.S.,Chatterjee, A.,Mittal, R.,Hosur, R.V. Effects of remote mutation on the autolysis of HIV-1 PR: X-ray and NMR investigations. Biochem.Biophys.Res.Commun., 294:395-401, 2002 Cited by PubMed Abstract: Autolysis rates of the C95M and C95M/C1095A mutants of a HIV-1 protease tethered dimer have been determined by real time NMR and it is observed that the double mutant has approximately two times higher rate. X-ray structure of the C95M/C1095A double mutant has been solved and refined to 2.1 A resolution. Comparison of the double mutant structure with that of C95M single mutant reveals that there is a shift in the position of the catalytic aspartates and the bound catalytic water. The mutation also causes a loss of hydrophobic packing near the dimerization domain of the protein. These observations demonstrate that subtle changes are adequate to cause significant changes in the rate of autolysis of the double mutant. This provides a rationale for the effects of remote mutations on the activity and drug resistance of the enzyme. PubMed: 12051725DOI: 10.1016/S0006-291X(02)00482-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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