2qsc

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(New page: 200px<br /><applet load="2qsc" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qsc, resolution 2.800&Aring;" /> '''Crystal structure a...)
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==Overview==
==Overview==
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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.
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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 Structure==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Bell, C.H.]]
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[[Category: Bell, C H.]]
[[Category: Schiefner, A.]]
[[Category: Schiefner, A.]]
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[[Category: Stanfield, R.L.]]
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[[Category: Stanfield, R L.]]
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[[Category: Wilson, I.A.]]
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[[Category: Wilson, I A.]]
[[Category: CL]]
[[Category: CL]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: virion]]
[[Category: virion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:08:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:41:53 2008''

Revision as of 16:41, 21 February 2008

Image:2qsc.jpg

2qsc, resolution 2.800Å

Drag the structure with the mouse to rotate

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

Overview

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 Structure

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

Reference

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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