2a55

From Proteopedia

(Difference between revisions)

Current revision

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

Structural highlights

2a55 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 40 models
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

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

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, 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jenkins HT, Mark L, Ball G, Persson J, Lindahl G, Uhrin D, Blom AM, Barlow PN. Human C4b-binding protein, structural basis for interaction with streptococcal M protein, a major bacterial virulence factor. J Biol Chem. 2006 Feb 10;281(6):3690-7. Epub 2005 Dec 5. PMID:16330538 doi:10.1074/jbc.M511563200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2a55"

@@ Line 1: / Line 1: @@
 ==Solution structure of the two N-terminal CCP modules of C4b-binding protein (C4BP) alpha-chain.==
-<StructureSection load='2a55' size='340' side='right' caption='[[2a55]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''>
+<StructureSection load='2a55' size='340' side='right'caption='[[2a55]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2a55]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A55 FirstGlance]. <br>
+<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>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C4BPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a55 OCA], [http://pdbe.org/2a55 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a55 RCSB], [http://www.ebi.ac.uk/pdbsum/2a55 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2a55 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=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>
 </table>
 == Function ==
-[[http://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.
+[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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 14: / Line 14: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a5/2a55_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Ball, G]]
+[[Category: Large Structures]]
-[[Category: Barlow, P N]]
+[[Category: Ball G]]
-[[Category: Blom, A M]]
+[[Category: Barlow PN]]
-[[Category: Jenkins, H T]]
+[[Category: Blom AM]]
-[[Category: Lindahl, G]]
+[[Category: Jenkins HT]]
-[[Category: Mark, L]]
+[[Category: Lindahl G]]
-[[Category: Uhrin, D]]
+[[Category: Mark L]]
-[[Category: Ccp module]]
+[[Category: Uhrin D]]
-[[Category: Complement]]
-[[Category: Immune system]]
-[[Category: Scr]]

2a55

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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