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| | <StructureSection load='2qy0' size='340' side='right'caption='[[2qy0]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='2qy0' size='340' side='right'caption='[[2qy0]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2qy0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QY0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2qy0]] 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=2QY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QY0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C1R ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Complement_subcomponent_C1r Complement subcomponent C1r], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.41 3.4.21.41] </span></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=2qy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qy0 OCA], [https://pdbe.org/2qy0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qy0 RCSB], [https://www.ebi.ac.uk/pdbsum/2qy0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qy0 ProSAT]</span></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=2qy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qy0 OCA], [https://pdbe.org/2qy0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qy0 RCSB], [https://www.ebi.ac.uk/pdbsum/2qy0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qy0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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.
| + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Complement subcomponent C1r]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Barabas, O]] | + | [[Category: Barabas O]] |
| - | [[Category: Gal, P]] | + | [[Category: Gal P]] |
| - | [[Category: Goto, Y]] | + | [[Category: Goto Y]] |
| - | [[Category: Graf, L]] | + | [[Category: Graf L]] |
| - | [[Category: Harmat, V]] | + | [[Category: Harmat V]] |
| - | [[Category: Kardos, J]] | + | [[Category: Kardos J]] |
| - | [[Category: Naray-Szabo, G]] | + | [[Category: Naray-Szabo G]] |
| - | [[Category: Pallo, A]] | + | [[Category: Pallo A]] |
| - | [[Category: Szilagyi, K]] | + | [[Category: Szilagyi K]] |
| - | [[Category: Zavodszky, P]] | + | [[Category: Zavodszky P]] |
| - | [[Category: Beta barrel]]
| + | |
| - | [[Category: Complement]]
| + | |
| - | [[Category: Complement pathway]]
| + | |
| - | [[Category: Egf-like domain]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Hydroxylation]]
| + | |
| - | [[Category: Immune response]]
| + | |
| - | [[Category: Innate immunity]]
| + | |
| - | [[Category: Phosphorylation]]
| + | |
| - | [[Category: Serine protease]]
| + | |
| - | [[Category: Sushi]]
| + | |
| Structural highlights
Function
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
C1r is a modular serine protease which is the autoactivating component of the C1 complex of the classical pathway of the complement system. We have determined the first crystal structure of the entire active catalytic region of human C1r. This fragment contains the C-terminal serine protease (SP) domain and the preceding two complement control protein (CCP) modules. The activated CCP1-CCP2-SP fragment makes up a dimer in a head-to-tail fashion similarly to the previously characterized zymogen. The present structure shows an increased number of stabilizing interactions. Moreover, in the crystal lattice there is an enzyme-product relationship between the C1r molecules of neighboring dimers. This enzyme-product complex exhibits the crucial S1-P1 salt bridge between Asp631 and Arg446 residues, and intermolecular interaction between the CCP2 module and the SP domain. Based on these novel structural information we propose a new split-and-reassembly model for the autoactivation of the C1r. This model is consistent with experimental results that have not been explained adequately by previous models. It allows autoactivation of C1r without large-scale, directed movement of C1q arms. The model is concordant with the stability of the C1 complex during activation of the next complement components.
Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: structure of the active catalytic region of C1r.,Kardos J, Harmat V, Pallo A, Barabas O, Szilagyi K, Graf L, Naray-Szabo G, Goto Y, Zavodszky P, Gal P Mol Immunol. 2008 Mar;45(6):1752-60. Epub 2007 Nov 9. PMID:17996945[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kardos J, Harmat V, Pallo A, Barabas O, Szilagyi K, Graf L, Naray-Szabo G, Goto Y, Zavodszky P, Gal P. Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: structure of the active catalytic region of C1r. Mol Immunol. 2008 Mar;45(6):1752-60. Epub 2007 Nov 9. PMID:17996945 doi:10.1016/j.molimm.2007.09.031
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