Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain
Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain
复制标题
DOI：
10.1016/s0092-8674(00)81276-3
复制
发表时间：
1996-06-14
期刊：
影响因子：
64.5
通讯作者：
Kuriyan, J
中科院分区：
文献类型：
--
作者：
Lee, CH;Saksela, K;Kuriyan, J
HIV-1 Nef保守核心的晶体结构已确定与突变体Fyn酪氨酸激酶（单氨基酸取代，Arg-96到异亮氨酸）的SH3结构域复合物，Nef与之紧密结合。Nef的保守PxxP序列基序，已知对最佳病毒复制很重要，是聚脯氨酸II型螺旋的一部分，以一种类似于分离肽与SH3结构域相互作用的方式参与SH3结构域。Nef-SH3结构也揭示了PxxP基序在Nef折叠结构背景下的呈现是如何在SH3相互作用中获得高亲和力和特异性的。
The crystal structure of the conserved core of HIV-1 Nef has been determined in complex with the SH3 domain of a mutant Fyn tyrosine kinase (a single amino acid substitution, Arg-96 to isoleucine), to which Nef binds tightly. The conserved PxxP sequence motif of Nef, known to be important for optimal viral replication, is part of a polyproline type II helix that engages the SH3 domain in a manner resembling closely the interaction of isolated peptides with SH3 domains. The Nef-SH3 structure also reveals how high affinity and specificity in the SH3 interaction is achieved by the presentation of the PxxP motif within the context of the folded structure of Nef.