Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV-1 gp120.
Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV-1 gp120.
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HIV-1 gp120 V3 环的抗体依赖性构象的固态 NMR 证据。
DOI：
10.1038/5827
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发表时间：
1999
期刊：
影响因子：
--
通讯作者：
Tycko,R
中科院分区：
文献类型：
--
作者：
Weliky,DP;Bennett,AE;Zvi,A;Anglister,J;Steinbach,PJ;Tycko,R
固态NMR测量已经进行了对来自HIV-1包膜糖蛋白gp 120的第三可变（V3）环的24-残基肽的复合物的冷冻溶液结合到抗gp 120抗体的Fab片段。测量对抗体结合状态下V3环的保守中心GPGR基序的构象有很强的约束。结合V3肽-抗体复合物的早期晶体结构和抗体交叉反应性的现有数据，固态NMR测量表明Gly-Pro-Gly-Arg（GPGR）基序在结合状态下采用抗体依赖性构象，并且在未结合的全长gp 120中可能是构象异质性的。这些测量是固态NMR方法在肽-蛋白质复合物结构研究中的首次应用。
Solid–state NMR measurements have been carried out on frozen solutions of the complex of a 24–residue peptide derived from the third variable (V3) loop of the HIV–1 envelope glycoprotein gp120 bound to the Fab fragment of an anti–gp120 antibody. The measurements place strong constraints on the conformation of the conserved central GPGR motif of the V3 loop in the antibody–bound state. In combination with earlier crystal structures of V3 peptide–antibody complexes and existing data on the cross–reactivity of the antibodies, the solid–state NMR measurements suggest that the Gly–Pro–Gly–Arg (GPGR) motif adopts an antibody–dependent conformation in the bound state and may be conformationally heterogeneous in unbound, full–length gp120. These measurements are the first application of solid–state NMR methods in a structural study of a peptide–protein complex.