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[[Image:1cd8.jpg|left|200px]]
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{{STRUCTURE_1cd8|  PDB=1cd8  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF A SOLUBLE FORM OF THE HUMAN T CELL CO-RECEPTOR CD8 AT 2.6 ANGSTROMS RESOLUTION'''


==CRYSTAL STRUCTURE OF A SOLUBLE FORM OF THE HUMAN T CELL CO-RECEPTOR CD8 AT 2.6 ANGSTROMS RESOLUTION==
<StructureSection load='1cd8' size='340' side='right'caption='[[1cd8]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1cd8]] 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=1CD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CD8 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1cd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cd8 OCA], [https://pdbe.org/1cd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cd8 RCSB], [https://www.ebi.ac.uk/pdbsum/1cd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cd8 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/CD8A_HUMAN CD8A_HUMAN] Defects in CD8A are a cause of familial CD8 deficiency (CD8 deficiency) [MIM:[https://omim.org/entry/608957 608957]. Familial CD8 deficiency is a novel autosomal recessive immunologic defect characterized by absence of CD8+ cells, leading to recurrent bacterial infections.
== Function ==
[https://www.uniprot.org/uniprot/CD8A_HUMAN CD8A_HUMAN] Identifies cytotoxic/suppressor T-cells that interact with MHC class I bearing targets. CD8 is thought to play a role in the process of T-cell mediated killing. CD8 alpha chains binds to class I MHC molecules alpha-3 domains.
== 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/cd/1cd8_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=1cd8 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A secreted fragment of the extracellular portion of human CD8 alpha has been expressed in CHO cells, and a deglycosylated and proteolyzed form of this fragment has been crystallized. We report here the crystal structure of this fragment as refined at 2.6 A resolution. The structure was solved by molecular replacement using a superposition of ten variable domains from immunoglobulin light chains as the search model. Only the N-terminal 114 amino acids of CD8 alpha are visible in the electron density maps. The domain formed by these residues possesses a fold typical of immunoglobulin variable domains and associates to form Fv-like homodimers.


==Overview==
Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 A resolution.,Leahy DJ, Axel R, Hendrickson WA Cell. 1992 Mar 20;68(6):1145-62. PMID:1547508<ref>PMID:1547508</ref>
A secreted fragment of the extracellular portion of human CD8 alpha has been expressed in CHO cells, and a deglycosylated and proteolyzed form of this fragment has been crystallized. We report here the crystal structure of this fragment as refined at 2.6 A resolution. The structure was solved by molecular replacement using a superposition of ten variable domains from immunoglobulin light chains as the search model. Only the N-terminal 114 amino acids of CD8 alpha are visible in the electron density maps. The domain formed by these residues possesses a fold typical of immunoglobulin variable domains and associates to form Fv-like homodimers.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1CD8 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CD8 OCA].
</div>
<div class="pdbe-citations 1cd8" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 A resolution., Leahy DJ, Axel R, Hendrickson WA, Cell. 1992 Mar 20;68(6):1145-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1547508 1547508]
*[[CD8 3D structures|CD8 3D structures]]
[[Category: Single protein]]
== References ==
[[Category: Axel, R.]]
<references/>
[[Category: Hendrickson, W A.]]
__TOC__
[[Category: Leahy, D J.]]
</StructureSection>
[[Category: Surface glycoprotein]]
[[Category: Homo sapiens]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:36:06 2008''
[[Category: Large Structures]]
[[Category: Axel R]]
[[Category: Hendrickson WA]]
[[Category: Leahy DJ]]
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