2qsc

File:2qsc.jpg

spinqualitylabelsall models 2qsc, resolution 2.800Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure analysis of anti-HIV-1 V3-Fab F425-B4e8 in complex with a V3-peptide

OverviewOverview

F425-B4e8 (B4e8) is a monoclonal antibody isolated from a human, immunodeficiency virus type 1 (HIV-1)-infected individual that recognizes, the V3 variable loop on the gp120 subunit of the viral envelope spike., B4e8 neutralizes a subset of HIV-1 primary isolates from subtypes B, C and, D, which places this antibody among the very few human anti-V3 antibodies, with notable cross-neutralizing activity. Here, the crystal structure of, the B4e8 Fab' fragment in complex with a 24-mer V3 peptide (RP142) at 2.8, A resolution is described. The complex structure reveals that the antibody, recognizes a novel V3 loop conformation, featuring a five-residue, alpha-turn around the conserved GPGRA apex of the beta-hairpin loop. In, agreement with previous mutagenesis analyses, the Fab' interacts primarily, with V3 through side-chain contacts with just two residues, Ile(P309) and, Arg(P315), while the remaining contacts are to the main chain. The, structure helps explain how B4e8 can tolerate a certain degree of sequence, variation within V3 and, hence, is able to neutralize an appreciable, number of different HIV-1 isolates.

About this StructureAbout this Structure

2QSC is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structure of antibody F425-B4e8 in complex with a V3 peptide reveals a new binding mode for HIV-1 neutralization., Bell CH, Pantophlet R, Schiefner A, Cavacini LA, Stanfield RL, Burton DR, Wilson IA, J Mol Biol. 2008 Jan 25;375(4):969-78. Epub 2007 Nov 13. PMID:18068724

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