2aw2
From Proteopedia
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| , resolution 2.80Å | |||||||
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| Ligands: | , , | ||||||
| Gene: | BTLA (Homo sapiens), TNFRSF14, HVEA, HVEM (Homo sapiens) | ||||||
| Related: | 1XAU, 1JMA
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 31 01:58:01 2008
