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1hnf

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[[Image:1hnf.jpg|left|200px]]<br /><applet load="1hnf" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hnf, resolution 2.5&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE EXTRACELLULAR REGION OF THE HUMAN CELL ADHESION MOLECULE CD2 AT 2.5 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE EXTRACELLULAR REGION OF THE HUMAN CELL ADHESION MOLECULE CD2 AT 2.5 ANGSTROMS RESOLUTION==
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BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule, implicated in immune responses in vivo. The extracellular regions of the, human and rat homologues of CD2 share only 45% sequence identity and bind, different protein ligands. Comparison of the human and rat soluble CD2, (sCD2) structures should provide insights into the structural basis of, cell surface recognition. RESULTS: We therefore determined the crystal, structure of a form of human sCD2 with single N-acetylglucosamine residues, at each glycosylation site to 2.5 A resolution with an R-factor of 19.3%., It is composed of two immunoglobulin superfamily domains similar to those, of rat sCD2, but the relative orientation of the domains in the two, homologues differs by up to 20 degrees. An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically, related human sCD2 molecules duplicates, in a different lattice, that, observed in the rat sCD2 crystals. CONCLUSIONS: Intramolecular flexibility, appears to be a conserved feature of CD2. The head-to-head interaction, between molecules represents a general model for interactions between, adhesion molecules of this structural class. Ligand specificity may be, influenced by the distribution of charged residues on the binding face.
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<StructureSection load='1hnf' size='340' side='right'caption='[[1hnf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hnf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HNF 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">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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=NA:SODIUM+ION'>NA</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=1hnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hnf OCA], [https://pdbe.org/1hnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hnf RCSB], [https://www.ebi.ac.uk/pdbsum/1hnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hnf 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/hn/1hnf_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=1hnf ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1HNF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HNF OCA].
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*[[CD2|CD2]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution., Bodian DL, Jones EY, Harlos K, Stuart DI, Davis SJ, Structure. 1994 Aug 15;2(8):755-66. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7994575 7994575]
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[[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: Bodian, D.L.]]
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[[Category: Bodian DL]]
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[[Category: Davis, S.J.]]
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[[Category: Davis SJ]]
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[[Category: Harlos, K.]]
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[[Category: Harlos K]]
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[[Category: Jones, E.Y.]]
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[[Category: Jones EY]]
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[[Category: Stuart, D.I.]]
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[[Category: Stuart DI]]
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[[Category: NA]]
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[[Category: NAG]]
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[[Category: t lymphocyte adhesion glycoprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:57:18 2008''
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Current revision

CRYSTAL STRUCTURE OF THE EXTRACELLULAR REGION OF THE HUMAN CELL ADHESION MOLECULE CD2 AT 2.5 ANGSTROMS RESOLUTION

PDB ID 1hnf

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