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PDBsum entry 1uos

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protein Protein-protein interface(s) links
Sugar-binding protein PDB id
1uos
Jmol
Contents
Protein chains
133 a.a. *
124 a.a. *
Waters ×320
* Residue conservation analysis
PDB id:
1uos
Name: Sugar-binding protein
Title: The crystal structure of the snake venom toxin convulxin
Structure: Convulxin alpha. Chain: a, c. Synonym: cvx alpha. Convulxin beta. Chain: b, d. Synonym: cvx beta
Source: Crotalus durissus terrificus. South american rattlesnake. Organism_taxid: 8732. Organism_taxid: 8732
Biol. unit: Octamer (from PDB file)
Resolution:
2.70Å     R-factor:   0.235     R-free:   0.263
Authors: T.Batuwangala,M.Leduc,J.M.Gibbins,C.Bon,E.Y.Jones
Key ref:
T.Batuwangala et al. (2004). Structure of the snake-venom toxin convulxin. Acta Crystallogr D Biol Crystallogr, 60, 46-53. PubMed id: 14684891 DOI: 10.1107/S0907444903021620
Date:
22-Sep-03     Release date:   14-Oct-03    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
O93426  (CVXA_CRODU) -  Snaclec convulxin subunit alpha
Seq:
Struc:
158 a.a.
133 a.a.
Protein chains
Pfam   ArchSchema ?
O93427  (CVXB_CRODU) -  Snaclec convulxin subunit beta
Seq:
Struc:
148 a.a.
124 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biochemical function     carbohydrate binding     1 term  

 

 
DOI no: 10.1107/S0907444903021620 Acta Crystallogr D Biol Crystallogr 60:46-53 (2004)
PubMed id: 14684891  
 
 
Structure of the snake-venom toxin convulxin.
T.Batuwangala, M.Leduc, J.M.Gibbins, C.Bon, E.Y.Jones.
 
  ABSTRACT  
 
Snake venoms contain a number of proteins that interact with components of the haemostatic system that promote or inhibit events leading to blood-clot formation. The snake-venom protein convulxin (Cvx) binds glycoprotein (GP) VI, the platelet receptor for collagen, and triggers signal transduction. Here, the 2.7 A resolution crystal structure of Cvx is presented. In common with other members of this snake-venom protein family, Cvx is an alphabeta-heterodimer and conforms to the C-type lectin-fold topology. Comparison with other family members allows a set of Cvx residues that form a concave surface to be putatively implicated in GPVI binding. Unlike other family members, with the exception of flavocetin-A (FL-A), Cvx forms an (alphabeta)(4) tetramer. This oligomeric structure is consistent with Cvx clustering GPVI molecules on the surface of platelets and as a result promoting signal transduction activity. The Cvx structure and the location of the putative binding sites suggest a model for this multimeric signalling assembly.
 
  Selected figure(s)  
 
Figure 3.
Figure 3 Analysis of the concave surface of Cvx. (a) Surface representation of the Cvx tetramer. (b) Orientation of the concave surface relative to the rest of the molecule. - and -subunits are coloured blue and red, respectively. The van der Waals surface of the -heterodimer is depicted in transparent grey and the concave surface with a transparent brown tint. Relative orientations of views are given. (c) Close-up view of the concave surface of the -heterodimer. Residues contributing to charged patches are indicated. (d) Schematic representation of the Cvx tetramer interaction with protein ligand at the cell surface. The Cvx tetramer is depicted as in Fig. 1-(a) with a 120° rotation about the horizontal. Ligand molecules interacting at each concave surface are depicted as transparent gold spheres. The cell surface is depicted in grey.
Figure 4.
Figure 4 Homology modelling and analysis of GPVI. (a) Sequence alignment between GPVI and Lir-1. (b) C^ trace of the GPVI model in coil representation; side chains of residues contributing to charged patches are drawn in ball-and-stick representation. (c) Surface representation of GPVI model showing distribution of electrostatic potential coloured in blue (positive) and red (negative) viewed in three orientations. The starting orientation is as in (b).
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2004, 60, 46-53) copyright 2004.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19495561 R.Doley, and R.M.Kini (2009).
Protein complexes in snake venom.
  Cell Mol Life Sci, 66, 2851-2871.  
18583525 A.A.Watson, J.A.Eble, and C.A.O'Callaghan (2008).
Crystal structure of rhodocytin, a ligand for the platelet-activating receptor CLEC-2.
  Protein Sci, 17, 1611-1616.
PDB code: 2vrp
17690106 J.F.Arthur, Y.Shen, M.L.Kahn, M.C.Berndt, R.K.Andrews, and E.E.Gardiner (2007).
Ligand binding rapidly induces disulfide-dependent dimerization of glycoprotein VI on the platelet plasma membrane.
  J Biol Chem, 282, 30434-30441.  
17367493 O.Berlanga, T.Bori-Sanz, J.R.James, J.Frampton, S.J.Davis, M.G.Tomlinson, and S.P.Watson (2007).
Glycoprotein VI oligomerization in cell lines and platelets.
  J Thromb Haemost, 5, 1026-1033.  
17635730 R.W.Farndale, D.A.Slatter, P.R.Siljander, and G.E.Jarvis (2007).
Platelet receptor recognition and cross-talk in collagen-induced activation of platelets.
  J Thromb Haemost, 5, 220-229.  
16014566 T.J.Kunicki, Y.Cheli, M.Moroi, and K.Furihata (2005).
The influence of N-linked glycosylation on the function of platelet glycoprotein VI.
  Blood, 106, 2744-2749.  
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.