==Crystal structure of the human BTLA-HVEM complex==

<StructureSection load='2aw2' size='340' side='right' caption='[[2aw2]], [[Resolution|resolution]] 2.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[2aw2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AW2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AW2 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aw2 OCA], [http://pdbe.org/2aw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2aw2 RCSB], [http://www.ebi.ac.uk/pdbsum/2aw2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2aw2 ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/BTLA_HUMAN BTLA_HUMAN]] Lymphocyte inhibitory receptor which inhibits lymphocytes during immune response.<ref>PMID:12796776</ref> [[http://www.uniprot.org/uniprot/TNR14_HUMAN TNR14_HUMAN]] Receptor for BTLA. Receptor for TNFSF14/LIGHT and homotrimeric TNFSF1/lymphotoxin-alpha. Involved in lymphocyte activation. Plays an important role in HSV pathogenesis because it enhanced the entry of several wild-type HSV strains of both serotypes into CHO cells, and mediated HSV entry into activated human T-cells.<ref>PMID:8898196</ref>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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<ref>PMID:16169851</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 2aw2" style="background-color:#fffaf0;"></div>

==See Also==

*[[Tumor necrosis factor receptor|Tumor necrosis factor receptor]]

== References ==

<references/>

[[Category: Human]]

[[Category: Compaan, D M]]

[[Category: Protein-protein complex]]

[[Category: Tnfrsf]]