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| [[Image:1apq.gif|left|200px]]<br />
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| <applet load="1apq" size="450" color="white" frame="true" align="right" spinBox="true"
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| caption="1apq" />
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| '''STRUCTURE OF THE EGF-LIKE MODULE OF HUMAN C1R, NMR, 19 STRUCTURES'''<br />
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| ==Overview== | | ==STRUCTURE OF THE EGF-LIKE MODULE OF HUMAN C1R, NMR, 19 STRUCTURES== |
| The calcium-dependent interaction between C1r and C1s, the two homologous, serine proteases of the first component of human complement C1, is, mediated by their N-terminal regions. The latter comprise an epidermal, growth factor (EGF)-like module exhibiting the consensus sequence, characteristic of Ca(2+)-binding EGF modules, surrounded by two CUB, modules. Due to its Ca2+ binding ability, the C1r EGF-like module, (C1r-EGF) is supposed to participate in the C1r-C1s interaction. An, additional interesting feature of C1r-EGF is the unusually large loop, connecting the first two conserved cysteine residues. The solution, structure of synthetic C1r-EGF (residues 123-175) has been determined, using nuclear magnetic resonance and combined simulated, annealing-restrained molecular dynamics calculations. The resulting family, of 19 structures is characterized by a well-ordered C-terminal part, (residues Cys 144-Ala174) with a backbone rmsd of 0.7 A and a disordered, N-terminal, including the large loop between the first two cysteines, (Cys129 and Cys144). This loop is known to be surface exposed and may be, expected to participate in domain-domain or protein-protein interactions., In its C-terminal part, C1r-EGF possesses the characteristic EGF fold with, a major and a minor beta-sheet. The latter comprises a beta-bulge, and, comparison with other EGF-like modules reveals the existence of two, distinct structural and sequential motifs in the bulged part. Additional, experiments in the presence of 80 mM Ca2+ did not show significant, structural variation of C1r-EGF, in keeping with previous observations on, blood-clotting factors IX and X.
| | <StructureSection load='1apq' size='340' side='right'caption='[[1apq]]' scene=''> |
| | | == Structural highlights == |
| ==About this Structure== | | <table><tr><td colspan='2'>[[1apq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1APQ FirstGlance]. <br> |
| 1APQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Complement_subcomponent_C1r Complement subcomponent C1r], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.41 3.4.21.41] Structure known Active Site: CAB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1APQ OCA].
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1apq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apq OCA], [https://pdbe.org/1apq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1apq RCSB], [https://www.ebi.ac.uk/pdbsum/1apq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1apq ProSAT]</span></td></tr> |
| ==Reference== | | </table> |
| Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family., Bersch B, Hernandez JF, Marion D, Arlaud GJ, Biochemistry. 1998 Feb 3;37(5):1204-14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9477945 9477945]
| | == Function == |
| [[Category: Complement subcomponent C1r]]
| | [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 == |
| | [[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/ap/1apq_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=1apq ConSurf]. |
| | <div style="clear:both"></div> |
| | __TOC__ |
| | </StructureSection> |
| [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| [[Category: Single protein]] | | [[Category: Large Structures]] |
| [[Category: Arlaud, G.J.]] | | [[Category: Arlaud GJ]] |
| [[Category: Bersch, B.]] | | [[Category: Bersch B]] |
| [[Category: Hernandez, J.F.]] | | [[Category: Hernandez J-F]] |
| [[Category: Marion, D.]] | | [[Category: Marion D]] |
| [[Category: calcium binding]]
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| [[Category: complement]]
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| [[Category: egf]]
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| [[Category: serine protease]]
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| ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:50:14 2007''
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