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1lqv

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[[Image:1lqv.jpg|left|200px]]
 
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==Crystal structure of the Endothelial protein C receptor with phospholipid in the groove in complex with Gla domain of protein C.==
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The line below this paragraph, containing "STRUCTURE_1lqv", creates the "Structure Box" on the page.
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<StructureSection load='1lqv' size='340' side='right'caption='[[1lqv]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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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]] 1.6&#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=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>
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{{STRUCTURE_1lqv| PDB=1lqv | SCENE= }}
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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=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>
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</table>
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'''Crystal structure of the Endothelial protein C receptor with phospholipid in the groove in complex with Gla domain of protein C.'''
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== Function ==
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[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.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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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.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lq/1lqv_consurf.spt"</scriptWhenChecked>
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1LQV is a [[Protein complex]] structure of sequences from [http://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].
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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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==Reference==
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</jmolCheckbox>
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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://www.ncbi.nlm.nih.gov/pubmed/12034704 12034704]
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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=1lqv ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Dauter, Z.]]
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[[Category: Dauter Z]]
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[[Category: Dongfeng, Q.]]
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[[Category: Dongfeng Q]]
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[[Category: Esmon, C T.]]
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[[Category: Esmon CT]]
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[[Category: Esmon, N L.]]
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[[Category: Esmon NL]]
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[[Category: Oganesyan, N.]]
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[[Category: Oganesyan N]]
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[[Category: Oganesyan, V.]]
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[[Category: Oganesyan V]]
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[[Category: Terzyan, S.]]
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[[Category: Terzyan S]]
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[[Category: Ca ion binding]]
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[[Category: Phospholipid binding groove]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:11:27 2008''
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Current revision

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

PDB ID 1lqv

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