CRYSTAL-STRUCTURE OF A HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 NEUTRALIZING ANTIBODY, 50.1, IN COMPLEX WITH ITS V3 LOOP PEPTIDE ANTIGEN

被引:223
作者
RINI, JM
STANFIELD, RL
STURA, EA
SALINAS, PA
PROFY, AT
WILSON, IA
机构
[1] SCRIPPS RES INST, DEPT MOLEC BIOL, LA JOLLA, CA 92037 USA
[2] REPLIGEN CORP, CAMBRIDGE, MA 02139 USA
关键词
HUMAN IMMUNODEFICIENCY VIRUS TYPE-1 NEUTRALIZATION; GP120; ANTIPEPTIDE ANTIBODY; PEPTIDE CONFORMATION;
D O I
10.1073/pnas.90.13.6325
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 angstrom 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-angstrom-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.
引用
收藏
页码:6325 / 6329
页数:5
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