X-ray crystal structure and dynamics reveal HIV-1 protease drug interactions

Yong Wang; Tamaria G. Dewdney; Zhigang Liu; Samuel J. Reiter; Joseph S. Brunzelle; Iulia A. Kovari; Ladislau C. Kovari

X-ray crystal structure and dynamics reveal HIV-1 protease drug interactions

Yong Wang, Tamaria G. Dewdney, Zhigang Liu, Samuel J. Reiter, Joseph S. Brunzelle, Iulia A. Kovari, Ladislau C. Kovari

Pharmacology

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

Abstract

The dynamic movement of HIV-1 protease is an important feature for inhibitor design. The wide-open form of multi-drug resistant HIV-1 protease solved by our group exhibits an increase in flap distance. Stabilizing the protease flaps could be a strategy to overcome drug resistance. A peptidic inhibitor stabilizing the protease-inhibitor complex and a structural novel inhibitor targeting the wide-open form protease have been identified as a new scaffold for drug development.

Original language	English (US)
Pages (from-to)	221-230
Number of pages	10
Journal	Studia Universitatis Babes-Bolyai Chemia
Issue number	3
State	Published - Sep 2011

Keywords

Drug design
HIV-1 protease
Multi-drug resistance

ASJC Scopus subject areas

Chemistry(all)

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Cite this

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abstract = "The dynamic movement of HIV-1 protease is an important feature for inhibitor design. The wide-open form of multi-drug resistant HIV-1 protease solved by our group exhibits an increase in flap distance. Stabilizing the protease flaps could be a strategy to overcome drug resistance. A peptidic inhibitor stabilizing the protease-inhibitor complex and a structural novel inhibitor targeting the wide-open form protease have been identified as a new scaffold for drug development.",

keywords = "Drug design, HIV-1 protease, Multi-drug resistance",

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language = "English (US)",

pages = "221--230",

journal = "Studia Universitatis Babes-Bolyai Chemia",

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AU - Wang, Yong

AU - Dewdney, Tamaria G.

AU - Liu, Zhigang

AU - Reiter, Samuel J.

AU - Brunzelle, Joseph S.

AU - Kovari, Iulia A.

AU - Kovari, Ladislau C.

PY - 2011/9

Y1 - 2011/9

N2 - The dynamic movement of HIV-1 protease is an important feature for inhibitor design. The wide-open form of multi-drug resistant HIV-1 protease solved by our group exhibits an increase in flap distance. Stabilizing the protease flaps could be a strategy to overcome drug resistance. A peptidic inhibitor stabilizing the protease-inhibitor complex and a structural novel inhibitor targeting the wide-open form protease have been identified as a new scaffold for drug development.

AB - The dynamic movement of HIV-1 protease is an important feature for inhibitor design. The wide-open form of multi-drug resistant HIV-1 protease solved by our group exhibits an increase in flap distance. Stabilizing the protease flaps could be a strategy to overcome drug resistance. A peptidic inhibitor stabilizing the protease-inhibitor complex and a structural novel inhibitor targeting the wide-open form protease have been identified as a new scaffold for drug development.

KW - Drug design

KW - HIV-1 protease

KW - Multi-drug resistance

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ER -

X-ray crystal structure and dynamics reveal HIV-1 protease drug interactions

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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