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PDBsum entry 1rid
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protein ligands Protein-protein interface(s) links
Immune system PDB id
1rid

 

 

 

 

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Contents
Protein chains
244 a.a. *
Ligands
IDS-SGN-IDS-SGN-
IDS-SGN-IDS-SGN ×2
Waters ×841
* Residue conservation analysis
Obsolete entry
PDB id:
1rid
Name: Immune system
Title: Vaccinia complement protein in complex with heparin
Structure: Complement control protein. Chain: a, b. Synonym: vcp, secretory protein 35, protein c3, 28 kda protein. Engineered: yes
Source: Vaccinia virus. Organism_taxid: 10254. Strain: wr. Gene: c3l. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Resolution:
2.10Å     R-factor:   0.206     R-free:   0.252
Authors: V.K.Ganesh,S.A.Smith,G.J.Kotwal,K.H.M.Murthy
Key ref:
V.K.Ganesh et al. (2004). Structure of vaccinia complement protein in complex with heparin and potential implications for complement regulation. Proc Natl Acad Sci U S A, 101, 8924-8929. PubMed id: 15178763 DOI: 10.1073/pnas.0400744101
Date:
17-Nov-03     Release date:   22-Jun-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
P10998  (VCP_VACCV) - 
Key:    Secondary structure

 

 
DOI no: 10.1073/pnas.0400744101 Proc Natl Acad Sci U S A 101:8924-8929 (2004)
PubMed id: 15178763  
 
 
Structure of vaccinia complement protein in complex with heparin and potential implications for complement regulation.
V.K.Ganesh, S.A.Smith, G.J.Kotwal, K.H.Murthy.
 
  ABSTRACT  
 
Vaccinia virus complement control protein (VCP), a homolog of the regulators of the complement activation family of proteins, inhibits complement activation through mechanisms similar to human fluid-phase complement regulators factor H and C4b-binding protein. VCP has a heparin-binding activity that assists vaccinia in host interactions. Interaction with cell-surface polyanions like heparin is centrally important in the functioning of fluid-phase complement regulators and is the basis of host-target discrimination by the alternative pathway. We report the structure of VCP in complex with a heparin decasaccharide, which reveals changes in VCP that might be pertinent to complement regulation. Properties that VCP shares with fluid-phase complement regulators suggest that such conformational changes may be of relevance in the functioning of other complement regulators. Additionally, comparison of VCP-heparin interactions with potentially similar interactions in factor H might enable understanding of the structural basis of familial hemolytic uremic syndrome, attributed to mutational disruption of heparin and C3b binding by factor H.
 
  Selected figure(s)  
 
Figure 1.
Fig. 1. VCP-heparin interactions. LIGPLOT (40) representation of VCP-heparin interaction (VCP-A/hepC). Heparin bonds are colored purple; protein bonds, gold. Carbon atoms are colored black, oxygen is red, nitrogen is blue, and sulfur is yellow. Hydrogen bonds are shown as dashed green lines, and hydrophobic contacts are shown as semicircle with lines. 		Figure 6.
Fig. 6. Residues that delimit motion. A surface representation of VCP SCR3 (light green) and SCR4 (light purple) is shown. Surface patches of residues, the mutation of which might result in altered motion, are colored magenta, with corresponding numbers of FH residues (Fig. 4) in parentheses.
 
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21213103 G.J.Kotwal (2010).
Influence of glycosylation and oligomerization of vaccinia virus complement control protein on level and pattern of functional activity and immunogenicity.
  Protein Cell, 1, 1084-1092.  
20033014 B.Borrell (2009).
Fraud rocks protein community.
  Nature, 462, 970.  
19946139 K.Van Vliet, M.R.Mohamed, L.Zhang, N.Y.Villa, S.J.Werden, J.Liu, and G.McFadden (2009).
Poxvirus proteomics and virus-host protein interactions.
  Microbiol Mol Biol Rev, 73, 730-749.  
19667083 M.K.Liszewski, M.K.Leung, R.Hauhart, C.J.Fang, P.Bertram, and J.P.Atkinson (2009).
Smallpox inhibitor of complement enzymes (SPICE): dissecting functional sites and abrogating activity.
  J Immunol, 183, 3150-3159.  
  18768877 M.K.Liszewski, P.Bertram, M.K.Leung, R.Hauhart, L.Zhang, and J.P.Atkinson (2008).
Smallpox inhibitor of complement enzymes (SPICE): regulation of complement activation on cells and mechanism of its cellular attachment.
  J Immunol, 181, 4199-4207.  
17089378 R.E.Saunders, C.Abarrategui-Garrido, V.Frémeaux-Bacchi, E.Goicoechea de Jorge, T.H.Goodship, M.López Trascasa, M.Noris, I.M.Ponce Castro, G.Remuzzi, S.Rodríguez de Córdoba, P.Sánchez-Corral, C.Skerka, P.F.Zipfel, and S.J.Perkins (2007).
The interactive Factor H-atypical hemolytic uremic syndrome mutation database and website: update and integration of membrane cofactor protein and Factor I mutations with structural models.
  Hum Mutat, 28, 222-234.  
17051152 A.Abdul Ajees, K.Gunasekaran, J.E.Volanakis, S.V.Narayana, G.J.Kotwal, and H.M.Murthy (2006).
The structure of complement C3b provides insights into complement activation and regulation.
  Nature, 444, 221-225.
PDB code: 2hr0
16473914 L.Zhang, and D.Morikis (2006).
Immunophysical properties and prediction of activities for vaccinia virus complement control protein and smallpox inhibitor of complement enzymes using molecular dynamics and electrostatics.
  Biophys J, 90, 3106-3119.  
16571823 O.B.Spiller, L.Mark, C.E.Blue, D.G.Proctor, J.A.Aitken, A.M.Blom, and D.J.Blackbourn (2006).
Dissecting the regions of virion-associated Kaposi's sarcoma-associated herpesvirus complement control protein required for complement regulation and cell binding.
  J Virol, 80, 4068-4078.  
16281287 R.E.Saunders, T.H.Goodship, P.F.Zipfel, and S.J.Perkins (2006).
An interactive web database of factor H-associated hemolytic uremic syndrome mutations: insights into the structural consequences of disease-associated mutations.
  Hum Mutat, 27, 21-30.  
16834555 R.Sasisekharan, R.Raman, and V.Prabhakar (2006).
Glycomics approach to structure-function relationships of glycosaminoglycans.
  Annu Rev Biomed Eng, 8, 181-231.  
16601698 T.S.Jokiranta, V.P.Jaakola, M.J.Lehtinen, M.Pärepalo, S.Meri, and A.Goldman (2006).
Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome.
  EMBO J, 25, 1784-1794.
PDB code: 2g7i
16023794 E.Ciulla, A.Emery, D.Konz, and J.Krushkal (2005).
Evolutionary history of orthopoxvirus proteins similar to human complement regulators.
  Gene, 355, 40-47.  
16160165 J.Mullick, J.Bernet, Y.Panse, S.Hallihosur, A.K.Singh, and A.Sahu (2005).
Identification of complement regulatory domains in vaccinia virus complement control protein.
  J Virol, 79, 12382-12393.  
16278650 R.Raman, S.Raguram, G.Venkataraman, J.C.Paulson, and R.Sasisekharan (2005).
Glycomics: an integrated systems approach to structure-function relationships of glycans.
  Nat Methods, 2, 817-824.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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