2a55

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[[Image:2a55.gif|left|200px]]
 
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==Solution structure of the two N-terminal CCP modules of C4b-binding protein (C4BP) alpha-chain.==
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The line below this paragraph, containing "STRUCTURE_2a55", creates the "Structure Box" on the page.
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<StructureSection load='2a55' size='340' side='right'caption='[[2a55]]' 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'>[[2a55]] 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=2A55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A55 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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, 40 models</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=2a55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a55 OCA], [https://pdbe.org/2a55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a55 RCSB], [https://www.ebi.ac.uk/pdbsum/2a55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a55 ProSAT]</span></td></tr>
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{{STRUCTURE_2a55| PDB=2a55 | SCENE= }}
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</table>
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== Function ==
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'''Solution structure of the two N-terminal CCP modules of C4b-binding protein (C4BP) alpha-chain.'''
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[https://www.uniprot.org/uniprot/C4BPA_HUMAN C4BPA_HUMAN] Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It interacts also with anticoagulant protein S and with serum amyloid P component.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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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/a5/2a55_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=2a55 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 ==
Human C4b-binding protein (C4BP) protects host tissue, and those pathogens able to hijack this plasma glycoprotein, from complement-mediated destruction. We now show that the first two complement control protein (CCP) modules of the C4BP alpha-chain, plus the four residues connecting them, are necessary and sufficient for binding a bacterial virulence factor, the Streptococcus pyogenes M4 (Arp4) protein. Structure determination by NMR reveals two tightly coupled CCP modules in an elongated arrangement within this region of C4BP. Chemical shift perturbation studies demonstrate that the N-terminal, hypervariable region of M4 binds to a site including strand 1 of CCP module 2. This interaction is accompanied by an intermodular reorientation within C4BP. We thus provide a detailed picture of an interaction whereby a pathogen evades complement.
Human C4b-binding protein (C4BP) protects host tissue, and those pathogens able to hijack this plasma glycoprotein, from complement-mediated destruction. We now show that the first two complement control protein (CCP) modules of the C4BP alpha-chain, plus the four residues connecting them, are necessary and sufficient for binding a bacterial virulence factor, the Streptococcus pyogenes M4 (Arp4) protein. Structure determination by NMR reveals two tightly coupled CCP modules in an elongated arrangement within this region of C4BP. Chemical shift perturbation studies demonstrate that the N-terminal, hypervariable region of M4 binds to a site including strand 1 of CCP module 2. This interaction is accompanied by an intermodular reorientation within C4BP. We thus provide a detailed picture of an interaction whereby a pathogen evades complement.
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==About this Structure==
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Human C4b-binding protein, structural basis for interaction with streptococcal M protein, a major bacterial virulence factor.,Jenkins HT, Mark L, Ball G, Persson J, Lindahl G, Uhrin D, Blom AM, Barlow PN J Biol Chem. 2006 Feb 10;281(6):3690-7. Epub 2005 Dec 5. PMID:16330538<ref>PMID:16330538</ref>
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2A55 is a [[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=2A55 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Human C4b-binding protein, structural basis for interaction with streptococcal M protein, a major bacterial virulence factor., Jenkins HT, Mark L, Ball G, Persson J, Lindahl G, Uhrin D, Blom AM, Barlow PN, J Biol Chem. 2006 Feb 10;281(6):3690-7. Epub 2005 Dec 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16330538 16330538]
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</div>
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<div class="pdbe-citations 2a55" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Ball, G.]]
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[[Category: Ball G]]
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[[Category: Barlow, P N.]]
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[[Category: Barlow PN]]
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[[Category: Blom, A M.]]
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[[Category: Blom AM]]
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[[Category: Jenkins, H T.]]
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[[Category: Jenkins HT]]
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[[Category: Lindahl, G.]]
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[[Category: Lindahl G]]
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[[Category: Mark, L.]]
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[[Category: Mark L]]
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[[Category: Uhrin, D.]]
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[[Category: Uhrin D]]
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[[Category: Ccp module]]
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[[Category: Complement]]
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[[Category: Scr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:37:03 2008''
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Current revision

Solution structure of the two N-terminal CCP modules of C4b-binding protein (C4BP) alpha-chain.

PDB ID 2a55

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