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PDBsum entry 2vrp
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Sugar binding protein
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PDB id
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2vrp
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References listed in PDB file
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Key reference
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Title
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Crystal structure of rhodocytin, A ligand for the platelet-Activating receptor clec-2.
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Authors
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A.A.Watson,
J.A.Eble,
C.A.O'Callaghan.
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Ref.
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Protein Sci, 2008,
17,
1611-1616.
[DOI no: ]
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PubMed id
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Abstract
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Binding of the snake venom protein rhodocytin to CLEC-2, a receptor on the
surface of human platelets, initiates a signaling cascade leading to platelet
activation and aggregation. We have previously solved the structure of CLEC-2.
The 2.4 A resolution crystal structure of rhodocytin presented here demonstrates
that it is the first snake venom or other C-type lectin-like protein to assemble
as a non-disulfide linked (alphabeta)(2) tetramer. Rhodocytin is highly adapted
for interaction with CLEC-2 and displays a concave binding surface, which is
highly complementary to the experimentally determined binding interface on
CLEC-2. Using computational dynamic methods, surface electrostatic charge and
hydrophobicity analyses, and protein-protein docking predictions, we propose
that the (alphabeta)(2) rhodocytin tetramer induces clustering of CLEC-2
receptors on the platelet surface, which will trigger major signaling events
resulting in platelet activation and aggregation.
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Figure 1.
Figure 1. Rhodocytin is an (  β)[2]
tetrameric C-type lectin-like snake venom protein. (A)
Rhodocytin forms a tetramer containing two copies of a disulfide
linked β-heterodimer,
whereas factor X-bp is dimeric, and convulxin is cyclic. - and
β-chains are colored yellow and pink, respectively. Disulfide
bonds in rhodocytin are colored green. (B) Each image represents
the molecular surface of one rhodocytin β-heterodimer
at the interface that forms the tetramer. In the upper panel,
the hydrophobic surface is colored green. In the lower panel,
negatively and positively charged regions are colored red and
blue, respectively, from –7 to +7 kTe. (C) Hydrogen bonds are
shown as broken blue lines between residues of the two -chains
within the rhodocytin tetramer. For clarity, one -chain is
colored yellow and the other red. For residues involved in
hydrogen bonds, carbon atoms are colored light blue, oxygen is
red, and nitrogen is dark blue.
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The above figure is
reprinted
by permission from the Protein Society:
Protein Sci
(2008,
17,
1611-1616)
copyright 2008.
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