1gya

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(New page: 200px<br /> <applet load="1gya" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gya" /> '''N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUC...)
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[[Image:1gya.gif|left|200px]]<br />
 
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<applet load="1gya" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gya" />
 
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'''N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUCTURES OF THE ADHESION DOMAIN OF HUMAN CD2'''<br />
 
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==Overview==
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==N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUCTURES OF THE ADHESION DOMAIN OF HUMAN CD2==
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The adhesion domain of human CD2 bears a single N-linked carbohydrate. The, solution structure of a fragment of CD2 containing the covalently bound, high-mannose N-glycan [-(N-acetylglucosamine)2-(mannose)5-8] was solved by, nuclear magnetic resonance. The stem and two of three branches of the, carbohydrate structure are well defined and the mobility of proximal, glycan residues is restricted. Mutagenesis of all residues in the vicinity, of the glycan suggests that the glycan is not a component of the CD2-CD58, interface; rather, the carbohydrate stabilizes the protein fold by, counterbalancing an unfavorable clustering of five positive charges, centered about lysine-61 of CD2.
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<StructureSection load='1gya' size='340' side='right'caption='[[1gya]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gya]] 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=1GYA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GYA FirstGlance]. <br>
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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, 18 models</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=1gya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gya OCA], [https://pdbe.org/1gya PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gya RCSB], [https://www.ebi.ac.uk/pdbsum/1gya PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gya ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CD2_HUMAN CD2_HUMAN] CD2 interacts with lymphocyte function-associated antigen (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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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/1gya_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1gya 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 ==
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The adhesion domain of human CD2 bears a single N-linked carbohydrate. The solution structure of a fragment of CD2 containing the covalently bound high-mannose N-glycan [-(N-acetylglucosamine)2-(mannose)5-8] was solved by nuclear magnetic resonance. The stem and two of three branches of the carbohydrate structure are well defined and the mobility of proximal glycan residues is restricted. Mutagenesis of all residues in the vicinity of the glycan suggests that the glycan is not a component of the CD2-CD58 interface; rather, the carbohydrate stabilizes the protein fold by counterbalancing an unfavorable clustering of five positive charges centered about lysine-61 of CD2.
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==About this Structure==
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Conformation and function of the N-linked glycan in the adhesion domain of human CD2.,Wyss DF, Choi JS, Li J, Knoppers MH, Willis KJ, Arulanandam AR, Smolyar A, Reinherz EL, Wagner G Science. 1995 Sep 1;269(5228):1273-8. PMID:7544493<ref>PMID:7544493</ref>
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1GYA 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GYA 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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Conformation and function of the N-linked glycan in the adhesion domain of human CD2., Wyss DF, Choi JS, Li J, Knoppers MH, Willis KJ, Arulanandam AR, Smolyar A, Reinherz EL, Wagner G, Science. 1995 Sep 1;269(5228):1273-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7544493 7544493]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 1gya" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Choi, J.S.]]
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[[Category: Wagner, G.]]
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[[Category: Wyss, D.F.]]
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[[Category: cell surface adhesion receptor]]
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[[Category: immunoglobulin superfamily v-set domain]]
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[[Category: t lymphocyte adhesion glycoprotein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:10:09 2007''
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==See Also==
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*[[CD2|CD2]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Choi JS]]
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[[Category: Wagner G]]
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[[Category: Wyss DF]]

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N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUCTURES OF THE ADHESION DOMAIN OF HUMAN CD2

PDB ID 1gya

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