1gyf
From Proteopedia
(New page: 200px<br /> <applet load="1gyf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gyf" /> '''GYF DOMAIN FROM HUMAN CD2BP2 PROTEIN'''<br ...) |
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| - | [[Image:1gyf.gif|left|200px]]<br /> | + | [[Image:1gyf.gif|left|200px]]<br /><applet load="1gyf" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1gyf" size=" | + | |
caption="1gyf" /> | caption="1gyf" /> | ||
'''GYF DOMAIN FROM HUMAN CD2BP2 PROTEIN'''<br /> | '''GYF DOMAIN FROM HUMAN CD2BP2 PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | T cell activation through the CD2 cell surface receptor is transmitted by | + | T cell activation through the CD2 cell surface receptor is transmitted by proline-rich sequences within its cytoplasmic tail. A membrane-proximal proline-rich tandem repeat, involved in cytokine production, is recognized by the intracellular CD2 binding protein CD2BP2. We solved the solution structure of the CD2 binding domain of CD2BP2, which we name the glycine-tyrosine-phenylalanine (GYF) domain. The GYF sequence is part of a structurally unique bulge-helix-bulge motif that constitutes the major binding site for the CD2 tail. A hydrophobic surface patch is created by motif residues that are highly conserved among a variety of proteins from diverse eukaryotic species. Thus, the architecture of the GYF domain may be widely used in protein-protein associations. |
==About this Structure== | ==About this Structure== | ||
| - | 1GYF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1GYF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1GYF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Freund, C.]] | [[Category: Freund, C.]] | ||
[[Category: Nishizawa, K.]] | [[Category: Nishizawa, K.]] | ||
| - | [[Category: Reinherz, E | + | [[Category: Reinherz, E L.]] |
[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
[[Category: adapter domain]] | [[Category: adapter domain]] | ||
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[[Category: t cell signaling]] | [[Category: t cell signaling]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:21 2008'' |
Revision as of 10:55, 21 February 2008
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GYF DOMAIN FROM HUMAN CD2BP2 PROTEIN
Overview
T cell activation through the CD2 cell surface receptor is transmitted by proline-rich sequences within its cytoplasmic tail. A membrane-proximal proline-rich tandem repeat, involved in cytokine production, is recognized by the intracellular CD2 binding protein CD2BP2. We solved the solution structure of the CD2 binding domain of CD2BP2, which we name the glycine-tyrosine-phenylalanine (GYF) domain. The GYF sequence is part of a structurally unique bulge-helix-bulge motif that constitutes the major binding site for the CD2 tail. A hydrophobic surface patch is created by motif residues that are highly conserved among a variety of proteins from diverse eukaryotic species. Thus, the architecture of the GYF domain may be widely used in protein-protein associations.
About this Structure
1GYF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences., Freund C, Dotsch V, Nishizawa K, Reinherz EL, Wagner G, Nat Struct Biol. 1999 Jul;6(7):656-60. PMID:10404223
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