1acy
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1acy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1acy OCA], [http://www.ebi.ac.uk/pdbsum/1acy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1acy RCSB]</span> | ||
}} | }} | ||
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[[Category: complex(antibody/hiv-1 fragment)]] | [[Category: complex(antibody/hiv-1 fragment)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:37:40 2008'' |
Revision as of 15:37, 30 March 2008
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| , resolution 3.0Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE PRINCIPAL NEUTRALIZING SITE OF HIV-1
Overview
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.
About this Structure
1ACY is a Protein complex structure of sequences from Human immunodeficiency virus type 1 (isolate mn) and Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the principal neutralization site of HIV-1., Ghiara JB, Stura EA, Stanfield RL, Profy AT, Wilson IA, Science. 1994 Apr 1;264(5155):82-5. PMID:7511253
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