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[[Image:1lqv.jpg|left|200px]]<br /><applet load="1lqv" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lqv, resolution 1.6&Aring;" />
'''Crystal structure of the Endothelial protein C receptor with phospholipid in the groove in complex with Gla domain of protein C.'''<br />


==Overview==
==Crystal structure of the Endothelial protein C receptor with phospholipid in the groove in complex with Gla domain of protein C.==
The endothelial cell protein C receptor (EPCR) shares approximately 20%, sequence identity with the major histocompatibility complex class 1/CD1, family of molecules, accelerates the thrombin-thrombomodulin-dependent, generation of activated protein C, a natural anticoagulant, binds to, activated neutrophils, and can undergo translocation from the plasma, membrane to the nucleus. Blocking protein C/activated protein C binding to, the receptor inhibits not only protein C activation but the ability of the, host to respond appropriately to bacterial challenge, exacerbating both, the coagulant and inflammatory responses. To understand how EPCR, accomplishes these multiple tasks, we solved the crystal structure of EPCR, alone and in complex with the phospholipid binding domain of protein C., The structures were strikingly similar to CD1d. A tightly bound, phospholipid resides in the groove typically involved in antigen, presentation. The protein C binding site is outside this conserved groove, and is distal from the membrane-spanning domain. Extraction of the lipid, resulted in loss of protein C binding, which could be restored by lipid, reconstitution. CD1d augments the immune response by presenting glycolipid, antigens. The EPCR structure is a model for how CD1d binds lipids and, further suggests additional potential functions for EPCR in immune, regulation, possibly including the anti-phospholipid syndrome.
<StructureSection load='1lqv' size='340' side='right'caption='[[1lqv]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 
== Structural highlights ==
==Disease==
<table><tr><td colspan='2'>[[1lqv]] is a 4 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=1LQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LQV FirstGlance]. <br>
Known diseases associated with this structure: Purpura fulminans, neonatal OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176860 176860]], Thrombophilia due to protein C deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=176860 176860]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CGU:GAMMA-CARBOXY-GLUTAMIC+ACID'>CGU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqv OCA], [https://pdbe.org/1lqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lqv RCSB], [https://www.ebi.ac.uk/pdbsum/1lqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lqv ProSAT]</span></td></tr>
1LQV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=NDG:'>NDG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=PTY:'>PTY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQV OCA].  
</table>
 
== Function ==
==Reference==
[https://www.uniprot.org/uniprot/EPCR_HUMAN EPCR_HUMAN] Binds activated protein C. Enhances protein C activation by the thrombin-thrombomodulin complex; plays a role in the protein C pathway controlling blood coagulation.
The crystal structure of the endothelial protein C receptor and a bound phospholipid., Oganesyan V, Oganesyan N, Terzyan S, Qu D, Dauter Z, Esmon NL, Esmon CT, J Biol Chem. 2002 Jul 12;277(28):24851-4. Epub 2002 May 28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12034704 12034704]
== 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/lq/1lqv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1lqv ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Dauter, Z.]]
[[Category: Dauter Z]]
[[Category: Dongfeng, Q.]]
[[Category: Dongfeng Q]]
[[Category: Esmon, C.T.]]
[[Category: Esmon CT]]
[[Category: Esmon, N.L.]]
[[Category: Esmon NL]]
[[Category: Oganesyan, N.]]
[[Category: Oganesyan N]]
[[Category: Oganesyan, V.]]
[[Category: Oganesyan V]]
[[Category: Terzyan, S.]]
[[Category: Terzyan S]]
[[Category: CA]]
[[Category: NAG]]
[[Category: NDG]]
[[Category: PTY]]
[[Category: ca ion binding]]
[[Category: gla (gamma-carboxyglutamic acid) residues]]
[[Category: phospholipid binding groove]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:20:00 2008''

Latest revision as of 06:06, 3 April 2024

Crystal structure of the Endothelial protein C receptor with phospholipid in the groove in complex with Gla domain of protein C.

1lqv, resolution 1.60Å

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