1ACY

CRYSTAL STRUCTURE OF THE PRINCIPAL NEUTRALIZING SITE OF HIV-1

Summary for 1ACY

• Entry DOI: 10.2210/pdb1acy/pdb
• Descriptor: IGG1-KAPPA 59.1 FAB (LIGHT CHAIN), IGG1-KAPPA 59.1 FAB (HEAVY CHAIN), HIV-1 GP120 (MN ISOLATE) (3 entities in total)
• Functional Keywords: complex(antibody-hiv-1 fragment), complex(antibody-hiv-1 fragment) complex, complex(antibody/hiv-1 fragment)
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cell membrane; Single-pass membrane protein (Potential): P01869; Transmembrane protein gp41: Virion membrane; Single-pass type I membrane protein. Surface protein gp120: Virion membrane; Peripheral membrane protein: P05877
• Total number of polymer chains: 3
• Total formula weight: 50697.83

Authors

Ghiara, J.B.,Wilson, I.A. (deposition date: 1994-02-10, release date: 1994-07-31, Last modification date: 2024-10-16)

Primary citation

Ghiara, J.B.,Stura, E.A.,Stanfield, R.L.,Profy, A.T.,Wilson, I.A.
Crystal structure of the principal neutralization site of HIV-1.
Science, 264:82-85, 1994

PubMed Abstract: The crystal structure of a complex between a 24-amino acid peptide from the third variable (V3) loop of human immunodeficiency virus-type 1 (HIV-1) gp 120 and the Fab fragment of a broadly neutralizing antibody (59.1) was determined to 3 angstrom resolution. The tip of the V3 loop containing the Gly-Pro-Gly-Arg-Ala-Phe sequence adopts a double-turn conformation, which may be the basis of its conservation in many HIV-1 isolates. A complete map of the HIV-1 principal neutralizing determinant was constructed by stitching together structures of V3 loop peptides bound to 59.1 and to an isolate-specific (MN) neutralizing antibody (50.1). Structural conservation of the overlapping epitopes suggests that this biologically relevant conformation could be of use in the design of synthetic vaccines and drugs to inhibit HIV-1 entry and virus-related cellular fusion.

PubMed: 7511253

Experimental method

X-RAY DIFFRACTION (3 Å)