2aw2
From Proteopedia
(New page: 200px<br /> <applet load="2aw2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aw2, resolution 2.80Å" /> '''Crystal structure o...) |
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| - | [[Image:2aw2.gif|left|200px]]<br /> | + | [[Image:2aw2.gif|left|200px]]<br /><applet load="2aw2" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2aw2" size=" | + | |
caption="2aw2, resolution 2.80Å" /> | caption="2aw2, resolution 2.80Å" /> | ||
'''Crystal structure of the human BTLA-HVEM complex'''<br /> | '''Crystal structure of the human BTLA-HVEM complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Five CD28-like proteins exert positive or negative effects on immune | + | 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== | ==About this Structure== | ||
| - | 2AW2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NI as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2AW2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NI:'>NI</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AW2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Compaan, D | + | [[Category: Compaan, D M.]] |
[[Category: Eaton, D.]] | [[Category: Eaton, D.]] | ||
| - | [[Category: Gonzalez, L | + | [[Category: Gonzalez, L C.]] |
| - | [[Category: Hymowitz, S | + | [[Category: Hymowitz, S G.]] |
| - | [[Category: Loyet, K | + | [[Category: Loyet, K M.]] |
[[Category: Tom, I.]] | [[Category: Tom, I.]] | ||
[[Category: NI]] | [[Category: NI]] | ||
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[[Category: tnfrsf]] | [[Category: tnfrsf]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:31:34 2008'' |
Revision as of 14:31, 21 February 2008
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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 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
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