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PDBsum entry 5fmw

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protein links
Structural protein PDB id
5fmw
Contents
Protein chains
(+ 16 more) 481 a.a.*
* C-alpha coords only
PDB id:
5fmw
Name: Structural protein
Title: The poly-c9 component of the complement membrane attack complex
Structure: Polyc9. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q, r, s, t, u, v
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: blood
Authors: N.V.Dudkina,B.A.Spicer,C.F.Reboul,P.J.Conroy,N.Lukoyanova,H.Elmlund, R.H.P.Law,S.M.Ekkel,S.C.Kondos,R.J.A.Goode,G.Ramm,J.C.Whisstock, H.R.Saibil,M.A.Dunstone
Key ref: N.V.Dudkina et al. (2016). Structure of the poly-C9 component of the complement membrane attack complex. Nat Commun, 7, 10588. PubMed id: 26841934 DOI: 10.1038/ncomms10588
Date:
10-Nov-15     Release date:   17-Feb-16    
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P02748  (CO9_HUMAN) -  Complement component C9 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
559 a.a.
481 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1038/ncomms10588 Nat Commun 7:10588 (2016)
PubMed id: 26841934  
 
 
Structure of the poly-C9 component of the complement membrane attack complex.
N.V.Dudkina, B.A.Spicer, C.F.Reboul, P.J.Conroy, N.Lukoyanova, H.Elmlund, R.H.Law, S.M.Ekkel, S.C.Kondos, R.J.Goode, G.Ramm, J.C.Whisstock, H.R.Saibil, M.A.Dunstone.
 
  ABSTRACT  
 
The membrane attack complex (MAC)/perforin-like protein complement component 9 (C9) is the major component of the MAC, a multi-protein complex that forms pores in the membrane of target pathogens. In contrast to homologous proteins such as perforin and the cholesterol-dependent cytolysins (CDCs), all of which require the membrane for oligomerisation, C9 assembles directly onto the nascent MAC from solution. However, the molecular mechanism of MAC assembly remains to be understood. Here we present the 8 Å cryo-EM structure of a soluble form of the poly-C9 component of the MAC. These data reveal a 22-fold symmetrical arrangement of C9 molecules that yield an 88-strand pore-forming β-barrel. The N-terminal thrombospondin-1 (TSP1) domain forms an unexpectedly extensive part of the oligomerisation interface, thus likely facilitating solution-based assembly. These TSP1 interactions may also explain how additional C9 subunits can be recruited to the growing MAC subsequent to membrane insertion.
 

 

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