1GGI

CRYSTAL STRUCTURE OF AN HIV-1 NEUTRALIZING ANTIBODY 50.1 IN COMPLEX WITH ITS V3 LOOP PEPTIDE ANTIGEN

1GGI の概要

• エントリーDOI: 10.2210/pdb1ggi/pdb
• 分子名称: IGG2A 50.1 FAB (LIGHT CHAIN), IGG2A 50.1 FAB (HEAVY CHAIN), HIV-1 V3 LOOP PEPTIDE ANTIGEN (3 entities in total)
• 機能のキーワード: immunoglobulin
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 99300.65

構造登録者

Stanfield, R.L.,Rini, J.M.,Wilson, I.A. (登録日: 1993-04-02, 公開日: 1993-10-31, 最終更新日: 2024-10-16)

主引用文献

Rini, J.M.,Stanfield, R.L.,Stura, E.A.,Salinas, P.A.,Profy, A.T.,Wilson, I.A.
Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50.1, in complex with its V3 loop peptide antigen.
Proc.Natl.Acad.Sci.USA, 90:6325-6329, 1993

PubMed Abstract: The crystal structure of the Fab fragment of a human immunodeficiency virus type 1 (HIV-1) neutralizing monoclonal antibody Fab has been determined at 2.8 A resolution in complex with a linear 16-residue peptide from the third hypervariable region (V3) of gp120. The first 9 residues of the peptide are ordered in the electron density maps, and their conformation is in partial agreement with the beta-strand-type II beta-turn structure predicted for this portion of the V3 loop. Notably, several of the peptide residues that are well conserved among different HIV-1 isolates contact a nonpolar 25-A-long groove in the antibody-combining site. The largely extended structure of the peptide differs from the beta-turns seen as the primary determinants in other published anti-peptide Fab structures. Analysis of the specific Fab-peptide interactions only partially explains the MN isolate specificity shown by this antibody.

PubMed: 8327513
DOI: 10.1073/pnas.90.13.6325

実験手法

X-RAY DIFFRACTION (2.8 Å)