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[[Image:1hng.jpg|left|200px]]
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{{STRUCTURE_1hng|  PDB=1hng  |  SCENE=  }}
'''CRYSTAL STRUCTURE AT 2.8 ANGSTROMS RESOLUTION OF A SOLUBLE FORM OF THE CELL ADHESION MOLECULE CD2'''


==CRYSTAL STRUCTURE AT 2.8 ANGSTROMS RESOLUTION OF A SOLUBLE FORM OF THE CELL ADHESION MOLECULE CD2==
<StructureSection load='1hng' size='340' side='right'caption='[[1hng]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hng]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HNG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hng OCA], [https://pdbe.org/1hng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hng RCSB], [https://www.ebi.ac.uk/pdbsum/1hng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hng ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CD2_RAT CD2_RAT] 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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hn/1hng_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1hng ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of a soluble form of the T lymphocyte antigen CD2 provides the first complete view of the extracellular region of a cell adhesion molecule. The topology of the molecule, which comprises two immunoglobulin-like domains, is the same as that of the first two domains of CD4 but the relative domain orientation is altered by a fairly flexible linker region. The putative ligand-binding beta-sheet forms a flat surface towards the top of the molecule. Crystal contacts between these surfaces suggest a plausible model for the adhesive interaction.


==Overview==
Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2.,Jones EY, Davis SJ, Williams AF, Harlos K, Stuart DI Nature. 1992 Nov 19;360(6401):232-9. PMID:1279440<ref>PMID:1279440</ref>
The crystal structure of a soluble form of the T lymphocyte antigen CD2 provides the first complete view of the extracellular region of a cell adhesion molecule. The topology of the molecule, which comprises two immunoglobulin-like domains, is the same as that of the first two domains of CD4 but the relative domain orientation is altered by a fairly flexible linker region. The putative ligand-binding beta-sheet forms a flat surface towards the top of the molecule. Crystal contacts between these surfaces suggest a plausible model for the adhesive interaction.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1HNG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HNG OCA].
</div>
<div class="pdbe-citations 1hng" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2., Jones EY, Davis SJ, Williams AF, Harlos K, Stuart DI, Nature. 1992 Nov 19;360(6401):232-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1279440 1279440]
*[[CD2|CD2]]
[[Category: Rattus norvegicus]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Davis, S J.]]
__TOC__
[[Category: Harlos, K.]]
</StructureSection>
[[Category: Jones, E Y.]]
[[Category: Large Structures]]
[[Category: Stuart, D I.]]
[[Category: Rattus rattus]]
[[Category: Williams, A F.]]
[[Category: Davis SJ]]
[[Category: T lymphocyte adhesion glycoprotein]]
[[Category: Harlos K]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:02:25 2008''
[[Category: Jones EY]]
[[Category: Stuart DI]]
[[Category: Williams AF]]

Latest revision as of 06:42, 30 October 2024

CRYSTAL STRUCTURE AT 2.8 ANGSTROMS RESOLUTION OF A SOLUBLE FORM OF THE CELL ADHESION MOLECULE CD2

1hng, resolution 2.80Å

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