Abstract
The crystal structure of the human immunodeficiency virus type 1 (HIV-1) neutralizing, murine Fab 83.1 in complex with an HIV-1 gp120 V3 peptide has been determined to 2.57 A resolution. The conformation of the V3 loop peptide in complex with Fab 83.1 is very similar to V3 conformations seen previously with two other neutralizing Fabs, 50.1 and 59.1. The repeated identification of this same V3 conformation in complex with three very different, neutralizing antibodies indicates that it is a highly preferred structure for V3 loops on some strains of the HIV-1 virus.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Crystallography, X-Ray
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HIV Antibodies / chemistry
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HIV Antibodies / immunology
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HIV Antibodies / metabolism*
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HIV Envelope Protein gp120 / chemistry*
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HIV Envelope Protein gp120 / metabolism
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HIV-1 / chemistry
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HIV-1 / metabolism*
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Humans
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Immunoglobulin Fab Fragments / chemistry
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Immunoglobulin Fab Fragments / immunology
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Immunoglobulin Fab Fragments / metabolism*
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Models, Molecular
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Molecular Sequence Data
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Neutralization Tests
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Peptide Fragments / chemistry*
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Peptide Fragments / metabolism
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Protein Conformation
Substances
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HIV Antibodies
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HIV Envelope Protein gp120
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HIV envelope protein gp120 (305-321)
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Immunoglobulin Fab Fragments
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Peptide Fragments