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Default Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV

Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV-1 gp120.

Related Articles Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV-1 gp120.

Nat Struct Biol. 1999 Feb;6(2):141-5

Authors: Weliky DP, Bennett AE, Zvi A, Anglister J, Steinbach PJ, Tycko R

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.

PMID: 10048925 [PubMed - indexed for MEDLINE]



Source: PubMed
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