2VRP

Structure of rhodocytin

Summary for 2VRP

• Entry DOI: 10.2210/pdb2vrp/pdb
• Descriptor: AGGRETIN ALPHA CHAIN, AGGRETIN BETA CHAIN, SODIUM ION, ... (5 entities in total)
• Functional Keywords: c-type lectin-like, sugar-binding protein, lectin, clec-2, venom, aggretin, sugar binding protein
• Biological source: CALLOSELASMA RHODOSTOMA (MALAYAN PIT VIPER); More
• Cellular location: Secreted: Q9I841 Q9I840
• Total number of polymer chains: 2
• Total formula weight: 30363.44

Authors

Watson, A.A.,O'Callaghan, C.A. (deposition date: 2008-04-09, release date: 2008-07-08, Last modification date: 2024-10-16)

Primary citation

Watson, A.A.,Eble, J.A.,O'Callaghan, C.A.
Crystal Structure of Rhodocytin, a Ligand for the Platelet-Activating Receptor Clec-2.
Protein Sci., 17:1611-, 2008

PubMed Abstract: 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.

PubMed: 18583525
DOI: 10.1110/PS.035568.108

Experimental method

X-RAY DIFFRACTION (2.41 Å)