1gyf

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[[Image:1gyf.gif|left|200px]]
 
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==GYF DOMAIN FROM HUMAN CD2BP2 PROTEIN==
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The line below this paragraph, containing "STRUCTURE_1gyf", creates the "Structure Box" on the page.
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<StructureSection load='1gyf' size='340' side='right'caption='[[1gyf]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1gyf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GYF FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gyf OCA], [https://pdbe.org/1gyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gyf RCSB], [https://www.ebi.ac.uk/pdbsum/1gyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gyf ProSAT]</span></td></tr>
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{{STRUCTURE_1gyf| PDB=1gyf | SCENE= }}
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</table>
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== Function ==
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'''GYF DOMAIN FROM HUMAN CD2BP2 PROTEIN'''
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[https://www.uniprot.org/uniprot/CD2B2_HUMAN CD2B2_HUMAN]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gy/1gyf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1gyf ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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.
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.
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==About this Structure==
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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<ref>PMID:10404223</ref>
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1GYF is a [[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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10404223 10404223]
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</div>
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<div class="pdbe-citations 1gyf" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Doetsch, V.]]
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[[Category: Doetsch V]]
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[[Category: Freund, C.]]
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[[Category: Freund C]]
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[[Category: Nishizawa, K.]]
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[[Category: Nishizawa K]]
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[[Category: Reinherz, E L.]]
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[[Category: Reinherz EL]]
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[[Category: Wagner, G.]]
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[[Category: Wagner G]]
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[[Category: Adapter domain]]
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[[Category: Proline-rich sequence recognition]]
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[[Category: T cell signaling]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:10:37 2008''
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Current revision

GYF DOMAIN FROM HUMAN CD2BP2 PROTEIN

PDB ID 1gyf

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