1md8

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{{Seed}}
 
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[[Image:1md8.png|left|200px]]
 
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==Monomeric structure of the active catalytic domain of complement protease C1r==
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The line below this paragraph, containing "STRUCTURE_1md8", creates the "Structure Box" on the page.
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<StructureSection load='1md8' size='340' side='right'caption='[[1md8]], [[Resolution|resolution]] 2.80&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'>[[1md8]] 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=1MD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MD8 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]] 2.8&#8491;</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=1md8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1md8 OCA], [https://pdbe.org/1md8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1md8 RCSB], [https://www.ebi.ac.uk/pdbsum/1md8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1md8 ProSAT]</span></td></tr>
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{{STRUCTURE_1md8| PDB=1md8 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/C1R_HUMAN C1R_HUMAN] C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system.
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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/md/1md8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1md8 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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C1r is the serine protease (SP) that mediates autoactivation of C1, the complex that triggers the classical complement pathway. We have determined the crystal structure of two fragments from the human C1r catalytic domain, each encompassing the second complement control protein (CCP2) module and the SP domain. The wild-type species has an active structure, whereas the S637A mutant is a zymogen. The structures reveal a restricted hinge flexibility of the CCP2-SP interface, and both are characterized by the unique alpha-helical conformation of loop E. The zymogen activation domain exhibits high mobility, and the active structure shows a restricted access to most substrate binding subsites. Further implications relevant to the C1r self-activation process are derived from protein-protein interactions in the crystals.
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===Monomeric structure of the active catalytic domain of complement protease C1r===
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Monomeric structures of the zymogen and active catalytic domain of complement protease c1r: further insights into the c1 activation mechanism.,Budayova-Spano M, Grabarse W, Thielens NM, Hillen H, Lacroix M, Schmidt M, Fontecilla-Camps JC, Arlaud GJ, Gaboriaud C Structure. 2002 Nov;10(11):1509-19. PMID:12429092<ref>PMID:12429092</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_12429092}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1md8" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12429092 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12429092}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1MD8 is a 1 chain structure of sequence 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=1MD8 OCA].
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==Reference==
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<ref group="xtra">PMID:12429092</ref><references group="xtra"/>
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[[Category: Complement subcomponent C1r]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Arlaud, G J.]]
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[[Category: Large Structures]]
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[[Category: Budayova-Spano, M.]]
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[[Category: Arlaud GJ]]
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[[Category: Fontecilla-Camps, J.]]
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[[Category: Budayova-Spano M]]
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[[Category: Gaboriaud, C.]]
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[[Category: Fontecilla-Camps J]]
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[[Category: Grabarse, W.]]
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[[Category: Gaboriaud C]]
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[[Category: Hillen, H.]]
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[[Category: Grabarse W]]
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[[Category: Lacroix, M.]]
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[[Category: Hillen H]]
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[[Category: Schmidt, M.]]
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[[Category: Lacroix M]]
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[[Category: Thielens, N M.]]
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[[Category: Schmidt M]]
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[[Category: Activation]]
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[[Category: Thielens NM]]
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[[Category: Complement]]
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[[Category: Innate immunity]]
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[[Category: Serine protease]]
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[[Category: Substrate specificity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 05:35:10 2009''
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Current revision

Monomeric structure of the active catalytic domain of complement protease C1r

PDB ID 1md8

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