1rzf

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Revision as of 15:21, 8 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1rzf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rzf, resolution 1.70Å" /> '''Crystal structure o...)
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File:1rzf.gif


1rzf, resolution 1.70Å

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Crystal structure of Human anti-HIV-1 GP120-reactive antibody E51

OverviewOverview

The conserved surface of the HIV-1 gp120 envelope glycoprotein that binds, to the HIV-1 coreceptor is protected from humoral recognition by multiple, layers of camouflage. Here we present sequence and genomic analyses for 12, antibodies that pierce these defenses and determine the crystal structures, of 5. The data reveal mechanisms and atomic-level details for three, unusual immune features: posttranslational mimicry of coreceptor by, tyrosine sulfation of antibody, an alternative molecular mechanism, controlling such sulfation, and highly selective V(H)-gene usage. When, confronted by extraordinary viral defenses, the immune system unveils, novel adaptive capabilities, with tyrosine sulfation enhancing the, vocabulary of antigen recognition.

About this StructureAbout this Structure

1RZF is a Protein complex structure of sequences from Homo sapiens with GOL and IPA as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120., Huang CC, Venturi M, Majeed S, Moore MJ, Phogat S, Zhang MY, Dimitrov DS, Hendrickson WA, Robinson J, Sodroski J, Wyatt R, Choe H, Farzan M, Kwong PD, Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):2706-11. Epub 2004 Feb 23. PMID:14981267

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