1lv1
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Autolysis rates of the C95M and C95M/C1095A mutants of a HIV-1 protease | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Human immunodeficiency virus 1]] | [[Category: Human immunodeficiency virus 1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bhavesh, N | + | [[Category: Bhavesh, N S.]] |
[[Category: Chatterjee, A.]] | [[Category: Chatterjee, A.]] | ||
| - | [[Category: Hosur, M | + | [[Category: Hosur, M V.]] |
| - | [[Category: Hosur, R | + | [[Category: Hosur, R V.]] |
| - | [[Category: Kannan, K | + | [[Category: Kannan, K K.]] |
[[Category: Kumar, M.]] | [[Category: Kumar, M.]] | ||
[[Category: Mittal, R.]] | [[Category: Mittal, R.]] | ||
[[Category: beta-ribbon flap]] | [[Category: beta-ribbon flap]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:47 2008'' |
Revision as of 11:48, 21 February 2008
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Crystal Structure Analysis of the non-active site mutant of tethered HIV-1 protease to 2.1A resolution
Overview
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.
About this Structure
1LV1 is a Single protein structure of sequence from Human immunodeficiency virus 1. Active as HIV-1 retropepsin, with EC number 3.4.23.16 Full crystallographic information is available from OCA.
Reference
Effects of remote mutation on the autolysis of HIV-1 PR: X-ray and NMR investigations., Kumar M, Kannan KK, Hosur MV, Bhavesh NS, Chatterjee A, Mittal R, Hosur RV, Biochem Biophys Res Commun. 2002 Jun 7;294(2):395-401. PMID:12051725
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