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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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<applet load="1ggi" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1ggi, resolution 2.8&Aring;" />
caption="1ggi, resolution 2.8&Aring;" />
'''CRYSTAL STRUCTURE OF AN HIV-1 NEUTRALIZING ANTIBODY 50.1 IN COMPLEX WITH ITS V3 LOOP PEPTIDE ANTIGEN'''<br />
'''CRYSTAL STRUCTURE OF AN HIV-1 NEUTRALIZING ANTIBODY 50.1 IN COMPLEX WITH ITS V3 LOOP PEPTIDE ANTIGEN'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1GGI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GGI OCA].
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1GGI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GGI OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8327513 8327513]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8327513 8327513]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Rini, J.M.]]
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[[Category: Rini, J M.]]
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[[Category: Stanfield, R.L.]]
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[[Category: Stanfield, R L.]]
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[[Category: Wilson, I.A.]]
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[[Category: Wilson, I A.]]
[[Category: immunoglobulin]]
[[Category: immunoglobulin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 14:04:32 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:49:51 2008''

Revision as of 10:49, 21 February 2008


1ggi, resolution 2.8Å

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 12:49:51 2008

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