2aw2

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[[Image:2aw2.gif|left|200px]]
[[Image:2aw2.gif|left|200px]]
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{{Structure
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|PDB= 2aw2 |SIZE=350|CAPTION= <scene name='initialview01'>2aw2</scene>, resolution 2.80&Aring;
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The line below this paragraph, containing "STRUCTURE_2aw2", creates the "Structure Box" on the page.
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|SITE=
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|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>
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|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])
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|DOMAIN=
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{{STRUCTURE_2aw2| PDB=2aw2 | SCENE= }}
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|RELATEDENTRY=[[1xau|1XAU]], [[1jma|1JMA]]
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|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>
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}}
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'''Crystal structure of the human BTLA-HVEM complex'''
'''Crystal structure of the human BTLA-HVEM complex'''
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[[Category: Loyet, K M.]]
[[Category: Loyet, K M.]]
[[Category: Tom, I.]]
[[Category: Tom, I.]]
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[[Category: igg domain]]
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[[Category: Igg domain]]
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[[Category: igi domain]]
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[[Category: Igi domain]]
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[[Category: protein-protein complex]]
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[[Category: Protein-protein complex]]
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[[Category: tnfrsf]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:32:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:58:01 2008''
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Revision as of 16:32, 3 May 2008

Image:2aw2.gif

Template:STRUCTURE 2aw2

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 Sat May 3 19:32:29 2008

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