2qqh

From Proteopedia

(Difference between revisions)

Revision as of 02:12, 16 November 2017

Structure of C8a-MACPF reveals mechanism of membrane attack in complement immune defense

Structural highlights

2qqh is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Gene:	C8A (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[CO8A_HUMAN] Defects in C8A are a cause of complement component 8 deficiency type 1 (C8D1) [MIM:613790]. A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis.

Function

[CO8A_HUMAN] Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C8A inserts into the target membrane, but does not form pores by itself.^[1] ^[2]

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

Membrane attack is important for mammalian immune defense against invading microorganisms and infected host cells. Proteins of the complement membrane attack complex (MAC) and the protein perforin share a common MACPF domain that is responsible for membrane insertion and pore formation. We determined the crystal structure of the MACPF domain of complement component C8alpha at 2.5 angstrom resolution and show that it is structurally homologous to the bacterial, pore-forming, cholesterol-dependent cytolysins. The structure displays two regions that (in the bacterial cytolysins) refold into transmembrane beta hairpins, forming the lining of a barrel pore. Local hydrophobicity explains why C8alpha is the first complement protein to insert into the membrane. The size of the MACPF domain is consistent with known C9 pore sizes. These data imply that these mammalian and bacterial cytolytic proteins share a common mechanism of membrane insertion.

Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense.,Hadders MA, Beringer DX, Gros P Science. 2007 Sep 14;317(5844):1552-4. PMID:17872444^[3]

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

References

↑ Steckel EW, York RG, Monahan JB, Sodetz JM. The eighth component of human complement. Purification and physicochemical characterization of its unusual subunit structure. J Biol Chem. 1980 Dec 25;255(24):11997-2005. PMID:7440581
↑ Hadders MA, Beringer DX, Gros P. Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense. Science. 2007 Sep 14;317(5844):1552-4. PMID:17872444 doi:317/5844/1552
↑ Hadders MA, Beringer DX, Gros P. Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense. Science. 2007 Sep 14;317(5844):1552-4. PMID:17872444 doi:317/5844/1552

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Structure of C8a-MACPF reveals mechanism of membrane attack in complement immune defense==
 <StructureSection load='2qqh' size='340' side='right' caption='[[2qqh]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C8A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2qqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qqh OCA], [http://pdbe.org/2qqh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qqh RCSB], [http://www.ebi.ac.uk/pdbsum/2qqh PDBsum]</span></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=2qqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qqh OCA], [http://pdbe.org/2qqh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qqh RCSB], [http://www.ebi.ac.uk/pdbsum/2qqh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qqh ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 51: / Line 52: @@
 [[Category: Membrane perforation]]
 [[Category: Membrane protein]]
+[[Category: Polymorphism]]
 [[Category: Secreted]]

2qqh

From Proteopedia

Revision as of 02:12, 16 November 2017

Structure of C8a-MACPF reveals mechanism of membrane attack in complement immune defense

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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