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人共激活因子CBP的KIX结构域与HIV-1 Tat相互作用表面的核磁共振图谱分析

NMR mapping of the HIV-1 Tat interaction surface of the KIX domain of the human coactivator CBP.

作者信息

Vendel Andrew C, Lumb Kevin J

机构信息

Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523-1870, USA.

出版信息

Biochemistry. 2004 Feb 3;43(4):904-8. doi: 10.1021/bi035612l.

DOI:10.1021/bi035612l
PMID:14744133
Abstract

Tat is required for the expression of the HIV-1 genome. HIV-1 Tat interacts with the human transcriptional coactivator and acetyltransferase CREB-binding protein (CBP) via the KIX domain of CBP. Chemical shift perturbation mapping with nuclear magnetic resonance spectroscopy was used to identify the surface of human KIX that interacts with Tat. It was found that Tat binds to the c-Jun/MLL/Tax binding surface of KIX, as opposed to the CREB binding site. The results provide new insight into the molecular basis of the assembly of protein complexes involving p300/CBP and Tat during HIV gene expression.

摘要

HIV-1基因组的表达需要Tat。HIV-1 Tat通过CBP的KIX结构域与人转录共激活因子及乙酰转移酶CREB结合蛋白(CBP)相互作用。利用核磁共振光谱进行化学位移扰动图谱分析,以确定人KIX与Tat相互作用的表面。结果发现,Tat与KIX的c-Jun/MLL/Tax结合表面结合,而非CREB结合位点。这些结果为HIV基因表达过程中涉及p300/CBP和Tat的蛋白质复合物组装的分子基础提供了新的见解。

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