3cyw: Difference between revisions

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[[Image:3cyw.jpg|left|200px]]
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[[Image:3cyw.png|left|200px]]


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{{STRUCTURE_3cyw|  PDB=3cyw  |  SCENE=  }}  
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'''Effect of Flap Mutations on Structure of HIV-1 Protease and Inhibition by Saquinavir and Darunavir'''
===Effect of Flap Mutations on Structure of HIV-1 Protease and Inhibition by Saquinavir and Darunavir===




==Overview==
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TMC114 (darunavir) is a promising clinical inhibitor of HIV-1 protease (PR) for treatment of drug resistant HIV/AIDS. We report the ultra-high 0.84 A resolution crystal structure of the TMC114 complex with PR containing the drug-resistant mutation V32I (PR(V32I)), and the 1.22 A resolution structure of a complex with PR(M46L). These structures show TMC114 bound at two distinct sites, one in the active-site cavity and the second on the surface of one of the flexible flaps in the PR dimer. Remarkably, TMC114 binds at these two sites simultaneously in two diastereomers related by inversion of the sulfonamide nitrogen. Moreover, the flap site is shaped to accommodate the diastereomer with the S-enantiomeric nitrogen rather than the one with the R-enantiomeric nitrogen. The existence of the second binding site and two diastereomers suggest a mechanism for the high effectiveness of TMC114 on drug-resistant HIV and the potential design of new inhibitors.
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{{ABSTRACT_PUBMED_18597780}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Effect of flap mutations on structure of HIV-1 protease and inhibition by saquinavir and darunavir., Liu F, Kovalevsky AY, Tie Y, Ghosh AK, Harrison RW, Weber IT, J Mol Biol. 2008 Aug 1;381(1):102-15. Epub 2008 Jul 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18597780 18597780]
Ultra-high resolution crystal structure of HIV-1 protease mutant reveals two binding sites for clinical inhibitor TMC114., Kovalevsky AY, Liu F, Leshchenko S, Ghosh AK, Louis JM, Harrison RW, Weber IT, J Mol Biol. 2006 Oct 13;363(1):161-73. Epub 2006 Aug 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16962136 16962136]
Ultra-high resolution crystal structure of HIV-1 protease mutant reveals two binding sites for clinical inhibitor TMC114., Kovalevsky AY, Liu F, Leshchenko S, Ghosh AK, Louis JM, Harrison RW, Weber IT, J Mol Biol. 2006 Oct 13;363(1):161-73. Epub 2006 Aug 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16962136 16962136]
Kinetic, stability, and structural changes in high-resolution crystal structures of HIV-1 protease with drug-resistant mutations L24I, I50V, and G73S., Liu F, Boross PI, Wang YF, Tozser J, Louis JM, Harrison RW, Weber IT, J Mol Biol. 2005 Dec 9;354(4):789-800. Epub 2005 Oct 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16277992 16277992]
[[Category: HIV-1 retropepsin]]
[[Category: HIV-1 retropepsin]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Human immunodeficiency virus 1]]
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[[Category: Zinc]]
[[Category: Zinc]]
[[Category: Zinc-finger]]
[[Category: Zinc-finger]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:24:51 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 16 08:50:12 2008''

Revision as of 05:50, 16 July 2008

File:3cyw.png

Template:STRUCTURE 3cyw

Effect of Flap Mutations on Structure of HIV-1 Protease and Inhibition by Saquinavir and Darunavir

Template:ABSTRACT PUBMED 18597780

About this Structure

3CYW is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

Effect of flap mutations on structure of HIV-1 protease and inhibition by saquinavir and darunavir., Liu F, Kovalevsky AY, Tie Y, Ghosh AK, Harrison RW, Weber IT, J Mol Biol. 2008 Aug 1;381(1):102-15. Epub 2008 Jul 1. PMID:18597780

Ultra-high resolution crystal structure of HIV-1 protease mutant reveals two binding sites for clinical inhibitor TMC114., Kovalevsky AY, Liu F, Leshchenko S, Ghosh AK, Louis JM, Harrison RW, Weber IT, J Mol Biol. 2006 Oct 13;363(1):161-73. Epub 2006 Aug 4. PMID:16962136

Kinetic, stability, and structural changes in high-resolution crystal structures of HIV-1 protease with drug-resistant mutations L24I, I50V, and G73S., Liu F, Boross PI, Wang YF, Tozser J, Louis JM, Harrison RW, Weber IT, J Mol Biol. 2005 Dec 9;354(4):789-800. Epub 2005 Oct 21. PMID:16277992

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