Crystal structure of a monomeric retroviral protease solved by protein folding game players

被引：274

作者：

Khatib, Firas ^{[1
]}

DiMaio, Frank ^{[1
]}

Cooper, Seth ^{[2
]}

Kazmierczyk, Maciej ^{[3
]}

Gilski, Miroslaw ^{[3
,6
]}

Krzywda, Szymon ^{[3
]}

Zabranska, Helena ^{[4
]}

Pichova, Iva ^{[4
]}

Thompson, James ^{[1
]}

Popovic, Zoran ^{[2
]}

Jaskolski, Mariusz ^{[3
,6
]}

Baker, David ^{[1
,5
]}

机构：

[1] Univ Washington, Dept Biochem, Seattle, WA 98195 USA

[2] Univ Washington, Dept Comp Sci & Engn, Seattle, WA 98195 USA

[3] Adam Mickiewicz Univ, Fac Chem, Dept Crystallog, Poznan, Poland

[4] Acad Sci Czech Republic, Inst Organ Chem & Biochem, Prague, Czech Republic

[5] Univ Washington, Howard Hughes Med Inst, Seattle, WA 98195 USA

[6] Polish Acad Sci, Inst Bioorgan Chem, Ctr Biocrystallog Res, Poznan, Poland

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2011年 / 18卷 / 10期

基金：

美国国家科学基金会;

关键词：

STRUCTURE PREDICTION; INHIBITORS;

D O I：

10.1038/nsmb.2119

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Following the failure of a wide range of attempts to solve the crystal structure of M-PMV retroviral protease by molecular replacement, we challenged players of the protein folding game Foldit to produce accurate models of the protein. Remarkably, Foldit players were able to generate models of sufficient quality for successful molecular replacement and subsequent structure determination. The refined structure provides new insights for the design of antiretroviral drugs.

引用

页码：1175 / 1177

页数：3