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3F58

IGG1 FAB FRAGMENT (58.2) COMPLEX WITH 12-RESIDUE CYCLIC PEPTIDE (INCLUDING RESIDUES 315-324 OF HIV-1 GP120 (MN ISOLATE); H315S MUTATION

Summary for 3F58
Entry DOI10.2210/pdb3f58/pdb
DescriptorPROTEIN (IMMUNOGLOBULIN GAMMA I (58.2)), PROTEIN (CYCLIC PEPTIDE (GP120)), ... (4 entities in total)
Functional Keywordsimmunoglobulin, fab, hiv-1, gp120, v3, immune system
Biological sourceMus musculus (house mouse)
More
Total number of polymer chains3
Total formula weight49342.75
Authors
Stanfield, R.L.,Cabezas, E.,Satterthwait, A.C.,Stura, E.A.,Profy, A.T.,Wilson, I.A. (deposition date: 1998-10-23, release date: 1999-02-09, Last modification date: 2024-11-20)
Primary citationStanfield, R.,Cabezas, E.,Satterthwait, A.,Stura, E.,Profy, A.,Wilson, I.
Dual conformations for the HIV-1 gp120 V3 loop in complexes with different neutralizing fabs.
Structure Fold.Des., 7:131-142, 1999
Cited by
PubMed Abstract: 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.
PubMed: 10368281
DOI: 10.1016/S0969-2126(99)80020-3
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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