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2aw2

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(New page: 200px<br /> <applet load="2aw2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aw2, resolution 2.80&Aring;" /> '''Crystal structure o...)
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Revision as of 18:48, 12 November 2007

Image:2aw2.gif

2aw2, resolution 2.80Å

Drag the structure with the mouse to rotate

Crystal structure of the human BTLA-HVEM complex

Overview

Five CD28-like proteins exert positive or negative effects on immune, cells. Only four of these five receptors interact with members of the B7, family. The exception is BTLA (B and T lymphocyte attenuator), which, instead interacts with the tumor necrosis factor receptor superfamily, member HVEM (herpes virus entry mediator). To better understand this, interaction, we determined the 2.8-A crystal structure of the BTLA-HVEM, complex. This structure shows that BTLA binds the N-terminal cysteine-rich, domain of HVEM and employs a unique binding surface compared with other, CD28-like receptors. Moreover, the structure shows that BTLA recognizes, the same surface on HVEM as gD (herpes virus glycoprotein D) and utilizes, a similar binding motif. Light scattering analysis demonstrates that the, extracellular domain of BTLA is monomeric and that BTLA and HVEM form a, 1:1 complex. Alanine-scanning mutagenesis of HVEM was used to further, define critical binding residues. Finally, BTLA adopts an immunoglobulin, I-set fold. Despite structural similarities to other CD28-like members, BTLA represents a unique co-receptor.

About this Structure

2AW2 is a Protein complex structure of sequences from Homo sapiens with NI as ligand. Full crystallographic information is available from OCA.

Reference

Attenuating lymphocyte activity: the crystal structure of the BTLA-HVEM complex., Compaan DM, Gonzalez LC, Tom I, Loyet KM, Eaton D, Hymowitz SG, J Biol Chem. 2005 Nov 25;280(47):39553-61. Epub 2005 Sep 16. PMID:16169851

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