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| [[Image:2q7z.gif|left|200px]]<br /><applet load="2q7z" size="350" color="white" frame="true" align="right" spinBox="true"
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| caption="2q7z" />
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| '''Solution Structure of the 30 SCR domains of human Complement Receptor 1'''<br />
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| ==Overview== | | ==Solution Structure of the 30 SCR domains of human Complement Receptor 1== |
| Human complement receptor type 1 (CR1, CD35) is a type I membrane-bound glycoprotein that belongs to the regulators of complement activity (RCA) family. The extra-cellular component of CR1 is comprised of 30 short complement regulator (SCR) domains, whereas complement receptor type 2 (CR2) has 15 SCR domains and factor H (FH) has 20 SCR domains. The domain arrangement of a soluble form of CR1 (sCR1) was studied by X-ray scattering and analytical ultracentrifugation. The radius of gyration R(G) of sCR1 of 13.4(+/-1.1) nm is not much greater than those for CR2 and FH, and its R(G)/R(0) anisotropy ratio is 3.76, compared to ratios of 3.67 for FH and 4.1 for CR2. Unlike CR2, but similar to FH, two cross-sectional R(G) ranges were identified that gave R(XS) values of 4.7(+/-0.2) nm and 1.2(+/-0.7) nm, respectively, showing that the SCR domains adopt a range of conformations including folded-back ones. The distance distribution function P(r) showed that the most commonly occurring distance in sCR1 is at 11.5 nm. Its maximum length of 55 nm is less than double those for CR2 or FH, even though sCR1 has twice the number of SCR domains compared to CR2 Sedimentation equilibrium experiments gave a mean molecular weight of 235 kDa for sCR1. This is consistent with the value of 245 kDa calculated from its composition including 14 N-linked oligosaccharide sites, and confirmed that sCR1 is a monomer in solution. Sedimentation velocity experiments gave a sedimentation coefficient of 5.8 S. From this, the frictional ratio (f/f(0)) of sCR1 was calculated to be 2.29, which is greater than those of 1.96 for CR2 and 1.77 for FH. The constrained scattering modelling of the sCR1 solution structure starting from homologous SCR domain structures generated 5000 trial conformationally randomised models, 43 of which gave good scattering fits to show that sCR1 has a partly folded-back structure. We conclude that the inter-SCR linkers show structural features in common with those in FH, but differ from those in CR2, and the SCR arrangement in CR1 will permit C3b or C4b to access all three ligand sites.
| | <StructureSection load='2q7z' size='340' side='right'caption='[[2q7z]]' scene=''> |
| | | == Structural highlights == |
| ==Disease== | | <table><tr><td colspan='2'>[[2q7z]] 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=2Q7Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q7Z FirstGlance]. <br> |
| Known diseases associated with this structure: Blood group, Knops system OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120620 120620]], CR1 deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120620 120620]], Malaria, severe, resistance to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120620 120620]], SLE susceptibility OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120620 120620]]
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray solution scattering</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=2q7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q7z OCA], [https://pdbe.org/2q7z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q7z RCSB], [https://www.ebi.ac.uk/pdbsum/2q7z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q7z ProSAT]</span></td></tr> |
| ==About this Structure== | | </table> |
| 2Q7Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] 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=2Q7Z OCA].
| | == Function == |
| | | [https://www.uniprot.org/uniprot/CR1_HUMAN CR1_HUMAN] Mediates cellular binding of particles and immune complexes that have activated complement. |
| ==Reference==
| | == Evolutionary Conservation == |
| The partly folded back solution structure arrangement of the 30 SCR domains in human complement receptor type 1 (CR1) permits access to its C3b and C4b ligands., Furtado PB, Huang CY, Ihyembe D, Hammond RA, Marsh HC, Perkins SJ, J Mol Biol. 2008 Jan 4;375(1):102-18. Epub 2007 Oct 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18028942 18028942]
| | [[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/q7/2q7z_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=2q7z ConSurf]. |
| | <div style="clear:both"></div> |
| | __TOC__ |
| | </StructureSection> |
| [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| [[Category: Single protein]] | | [[Category: Large Structures]] |
| [[Category: Furtado, P B.]] | | [[Category: Furtado PB]] |
| [[Category: Hammond, R A.]] | | [[Category: Hammond RA]] |
| [[Category: Huang, C Y.]] | | [[Category: Huang CY]] |
| [[Category: Ihyembe, D.]] | | [[Category: Ihyembe D]] |
| [[Category: Marsh, H C.]] | | [[Category: Marsh HC]] |
| [[Category: Perkins, S J.]] | | [[Category: Perkins SJ]] |
| [[Category: blood group antigen]]
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| [[Category: complement]]
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| [[Category: complement pathway]]
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| [[Category: glycoprotein]]
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| [[Category: immune response]]
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| [[Category: immune system]]
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| [[Category: innate immunity]]
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| [[Category: membrane]]
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| [[Category: polymorphism]]
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| [[Category: pyrrolidone carboxylic acid]]
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| [[Category: receptor]]
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| [[Category: scr domain]]
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| [[Category: sushi]]
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| [[Category: transmembrane]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:36:56 2008''
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