Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr

被引：119

作者：

Dieckmann, T

Withers-Ward, ES

Jarosinski, MA

Liu, CF

Chen, ISY

Feigon, J ^{[1
]}

机构：

[1] Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA

[2] Univ Calif Los Angeles, Inst Mol Biol, Los Angeles, CA 90095 USA

[3] Univ Calif Los Angeles, Dept Microbiol & Immunol, Los Angeles, CA 90095 USA

[4] Univ Calif Los Angeles, Dept Med, Los Angeles, CA 90095 USA

[5] Univ Calif Los Angeles, AIDS Inst, Los Angeles, CA 90095 USA

[6] Amgen Inc, Boulder, CO 80301 USA

[7] Dept DNA & Peptide Chem, Boulder, CO 80301 USA

来源：

NATURE STRUCTURAL BIOLOGY | 1998年 / 5卷 / 12期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1038/4220

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

The HIV-1 protein Vpr is critical for a number of viral functions including a unique ability to arrest T-cells at a G2/M checkpoint and induce subsequent apoptosis. It has been shown to interact specifically with the second UBA (ubiquitin associated) domain found in the DNA repair protein HHR23A, a highly evolutionarily conserved protein. This domain is a commonly occurring sequence motif in some members of the ubiquitination pathway, UV excision repair proteins, and certain protein kinases, The three dimensional structure of the UBA domain, determined by NMR spectroscopy, is presented. The protein domain forms a compact three-helix bundle. One side of the protein has a hydrophobic surface that is the most likely Vpr target site.

引用

页码：1042 / 1047

页数：6

共 31 条

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