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[[Image:2aw2.gif|left|200px]]


{{Structure
==Crystal structure of the human BTLA-HVEM complex==
|PDB= 2aw2 |SIZE=350|CAPTION= <scene name='initialview01'>2aw2</scene>, resolution 2.80&Aring;
<StructureSection load='2aw2' size='340' side='right'caption='[[2aw2]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <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>
<table><tr><td colspan='2'>[[2aw2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2AW2 FirstGlance]. <br>
|ACTIVITY=
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
|GENE= BTLA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), TNFRSF14, HVEA, HVEM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aw2 OCA], [https://pdbe.org/2aw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aw2 RCSB], [https://www.ebi.ac.uk/pdbsum/2aw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aw2 ProSAT]</span></td></tr>
|RELATEDENTRY=[[1xau|1XAU]], [[1jma|1JMA]]
</table>
|RESOURCES=<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://www.ebi.ac.uk/pdbsum/2aw2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2aw2 RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/BTLA_HUMAN BTLA_HUMAN] Lymphocyte inhibitory receptor which inhibits lymphocytes during immune response.<ref>PMID:12796776</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aw/2aw2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2aw2 ConSurf].
<div style="clear:both"></div>
<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.


'''Crystal structure of the human BTLA-HVEM complex'''
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>


==Overview==
==See Also==
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.
*[[Tumor necrosis factor receptor 3D structures|Tumor necrosis factor receptor 3D structures]]
 
== References ==
==About this Structure==
<references/>
2AW2 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AW2 OCA].
__TOC__
 
</StructureSection>
==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:[http://www.ncbi.nlm.nih.gov/pubmed/16169851 16169851]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Compaan, D M.]]
[[Category: Compaan DM]]
[[Category: Eaton, D.]]
[[Category: Eaton D]]
[[Category: Gonzalez, L C.]]
[[Category: Gonzalez LC]]
[[Category: Hymowitz, S G.]]
[[Category: Hymowitz SG]]
[[Category: Loyet, K M.]]
[[Category: Loyet KM]]
[[Category: Tom, I.]]
[[Category: Tom I]]
[[Category: igg domain]]
[[Category: igi domain]]
[[Category: protein-protein complex]]
[[Category: tnfrsf]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:58:01 2008''

Latest revision as of 07:50, 30 October 2024

Crystal structure of the human BTLA-HVEM complex

2aw2, resolution 2.80Å

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