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1f58

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[[Image:1f58.gif|left|200px]]
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[[Image:1f58.png|left|200px]]
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{{STRUCTURE_1f58| PDB=1f58 | SCENE= }}
{{STRUCTURE_1f58| PDB=1f58 | SCENE= }}
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'''IGG1 FAB FRAGMENT (58.2) COMPLEX WITH 24-RESIDUE PEPTIDE (RESIDUES 308-333 OF HIV-1 GP120 (MN ISOLATE) WITH ALA TO AIB SUBSTITUTION AT POSITION 323'''
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===IGG1 FAB FRAGMENT (58.2) COMPLEX WITH 24-RESIDUE PEPTIDE (RESIDUES 308-333 OF HIV-1 GP120 (MN ISOLATE) WITH ALA TO AIB SUBSTITUTION AT POSITION 323===
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==Overview==
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BACKGROUND: The third hypervariable (V3) loop of HIV-1 gp120 has been termed the principal neutralizing determinant (PND) of the virus and is involved in many aspects of virus infectivity. The V3 loop is required for viral entry into the cell via membrane fusion and is believed to interact with cell surface chemokine receptors on T cells and macrophages. Sequence changes in V3 can affect chemokine receptor usage, and can, therefore, modulate which types of cells are infected. Antibodies raised against peptides with V3 sequences can neutralize laboratory-adapted strains of the virus and inhibit syncytia formation. Fab fragments of these neutralizing antibodies in complex with V3 loop peptides have been studied by X-ray crystallography to determine the conformation of the V3 loop. RESULTS: We have determined three crystal structures of Fab 58.2, a broadly neutralizing antibody, in complex with one linear and two cyclic peptides the amino acid sequence of which comes from the MN isolate of the gp120 V3 loop. Although the peptide conformations are very similar for the linear and cyclic forms, they differ from that seen for the identical peptide bound to a different broadly neutralizing antibody, Fab 59.1, and for a similar peptide bound to the MN-specific Fab 50.1. The conformational difference in the peptide is localized around residues Gly-Pro-Gly-Arg, which are highly conserved in different HIV-1 isolates and are predicted to adopt a type II beta turn. CONCLUSIONS: The V3 loop can adopt at least two different conformations for the highly conserved Gly-Pro-Gly-Arg sequence at the tip of the loop. Thus, the HIV-1 V3 loop has some inherent conformational flexibility that may relate to its biological function.
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(as it appears on PubMed at http://www.pubmed.gov), where 10368281 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10368281}}
==About this Structure==
==About this Structure==
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[[Category: Immunoglobulin]]
[[Category: Immunoglobulin]]
[[Category: V3]]
[[Category: V3]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:55:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:42:57 2008''

Revision as of 23:42, 30 June 2008

Image:1f58.png

Template:STRUCTURE 1f58

IGG1 FAB FRAGMENT (58.2) COMPLEX WITH 24-RESIDUE PEPTIDE (RESIDUES 308-333 OF HIV-1 GP120 (MN ISOLATE) WITH ALA TO AIB SUBSTITUTION AT POSITION 323

Template:ABSTRACT PUBMED 10368281

About this Structure

1F58 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Dual conformations for the HIV-1 gp120 V3 loop in complexes with different neutralizing fabs., Stanfield R, Cabezas E, Satterthwait A, Stura E, Profy A, Wilson I, Structure. 1999 Feb 15;7(2):131-42. PMID:10368281

Page seeded by OCA on Tue Jul 1 02:42:57 2008

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