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J Biol Chem. 2010 Jan 8;285(2):1122-7. doi: 10.1074/jbc.M109.058792. Epub 2009 Nov 10.

Proline is not uniquely capable of providing the pivot point for domain swapping in 2G12, a broadly neutralizing antibody against HIV-1.

Author information

1
Department of Biotechnology, University of Natural Resources and Applied Life Sciences, 1190 Vienna, Austria. jgach@scripps-edu

Abstract

The human monoclonal antibody 2G12 is a member of a small group of broadly neutralizing antibodies against human immunodeficiency virus type 1. 2G12 adopts a unique variable heavy domain-exchanged dimeric configuration that results in an extensive multivalent binding surface and the ability to bind with high affinity to densely clustered high mannose oligosaccharides on the "silent" face of the gp120 envelope glycoprotein. Here, we further define the amino acids responsible for this extraordinary domain-swapping event in 2G12.

PMID:
19903812
PMCID:
PMC2801240
DOI:
10.1074/jbc.M109.058792
[Indexed for MEDLINE]
Free PMC Article

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