Structural basis of HIV-1 resistance to AZT by excision

被引：0

作者：

Xiongying Tu

Kalyan Das

Qianwei Han

Joseph D Bauman

Arthur D Clark

Xiaorong Hou

Yulia V Frenkel

Barbara L Gaffney

Roger A Jones

Paul L Boyer

Stephen H Hughes

Stefan G Sarafianos

Eddy Arnold

机构：

[1] Center for Advanced Biotechnology and Medicine,Department of Chemistry and Biology

[2] Rutgers University,undefined

[3] HIV Drug Resistance Program,undefined

[4] National Cancer Institute–Frederick,undefined

[5] Present address: Department of Molecular Microbiology & Immunology,undefined

[6] University of Missouri,undefined

[7] Columbia,undefined

[8] Missouri,undefined

[9] USA.,undefined

来源：

Nature Structural & Molecular Biology | 2010年 / 17卷

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摘要：

AZT is a nucleoside analog drug that inhibits HIV-1 reverse transcriptase (RT). The viral enzyme can acquire AZT resistance by mutations that enhance the rate of ATP-mediated excision of the incorporated AZT. Now structural work illustrates how the AZT resistance mutations create a high-affinity binding site for ATP and thus promote excision.

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页码：1202 / 1209

页数：7

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