Weliky D P, Bennett A E, Zvi A, Anglister J, Steinbach P J, Tycko R
Department of Chemistry, Michigan State University, East Lansing 48824, USA.
Nat Struct Biol. 1999 Feb;6(2):141-5. doi: 10.1038/5827.
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.
对源自HIV-1包膜糖蛋白gp120第三可变区（V3）环的24个残基肽与抗gp120抗体的Fab片段形成的复合物的冷冻溶液进行了固态核磁共振测量。这些测量对抗体结合状态下V3环保守的中央GPGR基序的构象施加了严格限制。结合V3肽-抗体复合物的早期晶体结构以及抗体交叉反应性的现有数据，固态核磁共振测量表明，甘氨酸-脯氨酸-甘氨酸-精氨酸（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gp120中可能在构象上是异质的。这些测量是固态核磁共振方法在肽-蛋白质复合物结构研究中的首次应用。
