HIV-1 Virus Interactions With Host Proteins: Interaction of the N-terminal Domain of the HIV-1 Capsid Protein With Human Calmodulin

被引：1
作者：
Tzou, Ywh-Min [1 ,2 ,3 ]
Shin, Ronald [1 ,2 ]
Krishna, N. Rama [1 ,2 ]
机构：
[1] Univ Alabama Birmingham, Dept Biochem & Mol Genet, Birmingham, AL 35294 USA
[2] Univ Alabama Birmingham, Comprehens Canc Ctr, Birmingham, AL 35294 USA
[3] Auburn Univ, Scott Ritchey Res Ctr, Coll Vet Med, Auburn, AL 36849 USA
来源：
NATURAL PRODUCT COMMUNICATIONS | 2019年 / 14卷 / 05期
基金：
美国国家卫生研究院;
关键词：
HIV-1; virus; calmodulin; capsid protein; N-terminal domain; ITC; NMR; CRYSTAL-STRUCTURE; BINDING DOMAIN; IDENTIFICATION; FLEXIBILITY; REGION; TYPE-1; VPR;
D O I：
10.1177/1934578X19849190
中图分类号：
R914 [药物化学];
学科分类号：
100701 ;
摘要：
The human immunodeficiency virus (HIV-1 virus) exploits several host factors for assembly, infection, and replication within the infected cells. In this work, we describe the evidence for an interaction of the N-terminal domain of the HIV-1 capsid protein with human calmodulin. The precise role of this interaction within the life cycle of the HIV-1 virus is yet to be defined. Potential roles for this interaction in the viral capsid uncoating are discussed.
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页数：6
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