1e5g

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(New page: 200px<br /><applet load="1e5g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e5g" /> '''SOLUTION STRUCTURE OF CENTRAL CP MODULE PAIR...)
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[[Image:1e5g.gif|left|200px]]<br /><applet load="1e5g" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1e5g" />
 
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'''SOLUTION STRUCTURE OF CENTRAL CP MODULE PAIR OF A POX VIRUS COMPLEMENT INHIBITOR'''<br />
 
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==Overview==
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==Solution structure of central CP module pair of a pox virus complement inhibitor==
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The complement control protein (CCP) module (also known as SCR, CCP or, sushi domain) is prevalent amongst proteins that regulate complement, activation. Functional and mutagenesis studies have shown that in most, cases two or more neighbouring CCP modules form specific binding sites for, other molecules. Hence the orientation in space of a CCP module with, respect to its neighbours and the flexibility of the intermodular junction, are likely to be critical for function. Vaccinia virus complement control, protein (VCP) is a complement regulatory protein composed of four tandemly, arranged CCP modules. The solution structure of the carboxy-terminal half, of this protein (CCP modules 3 and 4) has been solved previously. The, structure of the central portion (modules 2 and 3, VCP approximately 2,3), has now also been solved using NMR spectroscopy at 37 degrees C. In, addition, the backbone dynamics of VCP approximately 2,3 have been, characterised by analysis of its (15)N relaxation parameters. Module 2 has, a typical CCP module structure while module 3 in the context of VCP, approximately 2,3 has some modest but significant differences in structure, and dynamics to module 3 within the 3,4 pair. Modules 2 and 3 do not share, an extensive interface, unlike modules 3 and 4. Only two possible NOEs, were identified between the bodies of the modules, but a total of 40 NOEs, between the short intermodular linker of VCP approximately 2,3 and the, bodies of the two modules determines a preferred, elongated, orientation, of the two modules in the calculated structures. The anisotropy of, rotational diffusion has been characterised from (15)N relaxation data, and this indicates that the time-averaged structure is more compact than, suggested by (1)H-(1)H NOEs. The data are consistent with the presence of, many intermodular orientations, some of which are kinked, undergoing, interconversion on a 10(-8)-10(-6) second time-scale. A reconstructed, representation of modules 2-4 allows visualisation of the spatial, arrangement of the 11 substitutions that occur in the more potent, complement inhibitor from Variola (small pox) virus.
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<StructureSection load='1e5g' size='340' side='right'caption='[[1e5g]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1e5g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vaccinia_virus_Copenhagen Vaccinia virus Copenhagen]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E5G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E5G FirstGlance]. <br>
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1E5G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E5G OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1e5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e5g OCA], [https://pdbe.org/1e5g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e5g RCSB], [https://www.ebi.ac.uk/pdbsum/1e5g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e5g ProSAT]</span></td></tr>
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==Reference==
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</table>
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Solution structure and dynamics of the central CCP module pair of a poxvirus complement control protein., Henderson CE, Bromek K, Mullin NP, Smith BO, Uhrin D, Barlow PN, J Mol Biol. 2001 Mar 16;307(1):323-39. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11243823 11243823]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/VCP_VACCC VCP_VACCC] Serves to protect the virus against complement attack by inhibiting both classical and alternative pathways of complement activation. Binds C3b and C4b.
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[[Category: Vaccinia virus]]
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== Evolutionary Conservation ==
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[[Category: Barlow, P.N.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Bromek, K.]]
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Check<jmol>
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[[Category: Henderson, C.E.]]
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<jmolCheckbox>
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[[Category: Mullin, N.P.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e5/1e5g_consurf.spt"</scriptWhenChecked>
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[[Category: Smith, B.O.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: Uhrin, D.]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: complement]]
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</jmolCheckbox>
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[[Category: modules]]
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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=1e5g ConSurf].
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[[Category: nmr]]
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<div style="clear:both"></div>
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[[Category: protein structure]]
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__TOC__
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[[Category: vaccinia virus]]
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</StructureSection>
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[[Category: Large Structures]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:47:07 2007''
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[[Category: Vaccinia virus Copenhagen]]
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[[Category: Barlow PN]]
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[[Category: Bromek K]]
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[[Category: Henderson CE]]
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[[Category: Mullin NP]]
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[[Category: Smith BO]]
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[[Category: Uhrin D]]

Current revision

Solution structure of central CP module pair of a pox virus complement inhibitor

PDB ID 1e5g

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