2aw2
From Proteopedia
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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
Page seeded by OCA on Mon Nov 12 20:55:15 2007
