STRUCTURE/FUNCTION OF HIV1 CAPSID/CYCLOPHILIN COMPLEX

HIV1 衣壳/亲环蛋白复合物的结构/功能

• 批准号: 2004960
• 负责人: WESLEY I. SUNDQUIST
• 金额: $ 20.24万
• 依托单位: UNIVERSITY OF UTAH
• 依托单位国家: 美国
• 财政年份: 1997
• 资助国家: 美国
• 起止时间: 1997-03-01 至 2002-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2004960
• 关键词: X ray crystallography; capsid; enzyme activity; gene mutation; human immunodeficiency virus 1; peptidylprolyl isomerase; protein structure function; tissue /cell culture; virus replication

DESCRIPTION: (Adapted from Investigator's Abstract) Recent work has shown that packaging of the cellular protein cyclophilin A plays an important role in HIV-1 replication. Cyclophilin A incorporates into HIV-1 virions by virtue of binding to CA. To understand this interaction, the investigator will determine the crystal structure of cyclophilin A bound to a truncated form of CA. The truncated form binds cyclophilin A with the same affinity as full-length CA, but is a monomer rather than a dimer. Preliminary results show co-crystals that diffract to 2.5 A. In addition, binding of cyclophilin to a capsid peptide will be characterized biochemically and structurally. In particular the conformation of Pro90 in CA bound to cyclophilin A suggests that this residue may act as a substrate for cyclophilin rotamase activity. Finally, genetic analysis of mutants of CA in an HIV provirus will be used to test models that arise from the CA and CA-cyclophilin structures.

描述：（改编自研究者摘要）最近的研究表明