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1ggi

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(New page: 200px<br /> <applet load="1ggi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ggi, resolution 2.8&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 11:58, 8 November 2007


1ggi, resolution 2.8Å

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

Overview

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.

About this Structure

1GGI is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50.1, in complex with its V3 loop peptide antigen., Rini JM, Stanfield RL, Stura EA, Salinas PA, Profy AT, Wilson IA, Proc Natl Acad Sci U S A. 1993 Jul 1;90(13):6325-9. PMID:8327513

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