Crystallization and preliminary structure determination of an intact human immunoglobulin, b12: an antibody that broadly neutralizes primary isolates of HIV-1

被引：43

作者：

Saphire, EO

Parren, PWHI

Barbas, CF

Burton, DR

Wilson, IA

机构：

[1] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA

[2] Scripps Res Inst, Dept Immunol, La Jolla, CA 92037 USA

[3] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2001年 / 57卷

关键词：

D O I：

10.1107/S0907444900017376

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

An intact human immunoglobulin with a full-length hinge has been crystallized for the first time in a form in which all of the Ig domains are ordered. The IgG1 antibody b12 is one of only three known monoclonal antibodies described that potently neutralize a broad range of HIV-1 primary isolates. It binds to an epitope overlapping the conserved CD4 binding site on the viral surface antigen gp120. Hexagonal crystals corresponding to space group R32 were grown from 0.8 M ammonium sulfate, with unit-cell parameters a = b = 271.3, c = 175.2 Angstrom and one molecule per asymmetric unit. The crystals diffract to 2.8 Angstrom and a preliminary molecular-replacement solution indicates that all 12 Ig domains of the antibody can be resolved.

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页码：168 / 171

页数：4

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