Molecular analysis of the interaction of the snake venom rhodocytin with the platelet receptor CLEC-2.
The Malayan pit viper, Calloselasma rhodostoma, produces a potent venom toxin, rhodocytin (aggretin) which causes platelet aggregation. Rhodocytin is a ligand for the receptor CLEC-2 on the surface of platelets. The interaction of these two molecules initiates a signaling pathway which results in pl...
| Main Authors: | , |
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| Format: | Journal article |
| Language: | English |
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2011
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| _version_ | 1826281135388229632 |
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| author | Watson, A O'Callaghan, C |
| author_facet | Watson, A O'Callaghan, C |
| author_sort | Watson, A |
| collection | OXFORD |
| description | The Malayan pit viper, Calloselasma rhodostoma, produces a potent venom toxin, rhodocytin (aggretin) which causes platelet aggregation. Rhodocytin is a ligand for the receptor CLEC-2 on the surface of platelets. The interaction of these two molecules initiates a signaling pathway which results in platelet activation and aggregation. We have previously solved the crystal structures of CLEC-2 and of rhodocytin, and have proposed models by which tetrameric rhodocytin may interact with either two monomers of CLEC-2, or with one or two copies of dimeric CLEC-2. In the current study we use a range of approaches to analyze the molecular interfaces and dynamics involved in the models of the interaction of rhodocytin with either one or two copies of dimeric CLEC-2, and their implications for clustering of CLEC-2 on the platelet surface. |
| first_indexed | 2024-03-07T00:24:15Z |
| format | Journal article |
| id | oxford-uuid:7d93a91b-f45e-447c-aabe-030811969116 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T00:24:15Z |
| publishDate | 2011 |
| record_format | dspace |
| spelling | oxford-uuid:7d93a91b-f45e-447c-aabe-0308119691162022-03-26T21:04:35ZMolecular analysis of the interaction of the snake venom rhodocytin with the platelet receptor CLEC-2.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:7d93a91b-f45e-447c-aabe-030811969116EnglishSymplectic Elements at Oxford2011Watson, AO'Callaghan, CThe Malayan pit viper, Calloselasma rhodostoma, produces a potent venom toxin, rhodocytin (aggretin) which causes platelet aggregation. Rhodocytin is a ligand for the receptor CLEC-2 on the surface of platelets. The interaction of these two molecules initiates a signaling pathway which results in platelet activation and aggregation. We have previously solved the crystal structures of CLEC-2 and of rhodocytin, and have proposed models by which tetrameric rhodocytin may interact with either two monomers of CLEC-2, or with one or two copies of dimeric CLEC-2. In the current study we use a range of approaches to analyze the molecular interfaces and dynamics involved in the models of the interaction of rhodocytin with either one or two copies of dimeric CLEC-2, and their implications for clustering of CLEC-2 on the platelet surface. |
| spellingShingle | Watson, A O'Callaghan, C Molecular analysis of the interaction of the snake venom rhodocytin with the platelet receptor CLEC-2. |
| title | Molecular analysis of the interaction of the snake venom rhodocytin with the platelet receptor CLEC-2. |
| title_full | Molecular analysis of the interaction of the snake venom rhodocytin with the platelet receptor CLEC-2. |
| title_fullStr | Molecular analysis of the interaction of the snake venom rhodocytin with the platelet receptor CLEC-2. |
| title_full_unstemmed | Molecular analysis of the interaction of the snake venom rhodocytin with the platelet receptor CLEC-2. |
| title_short | Molecular analysis of the interaction of the snake venom rhodocytin with the platelet receptor CLEC-2. |
| title_sort | molecular analysis of the interaction of the snake venom rhodocytin with the platelet receptor clec 2 |
| work_keys_str_mv | AT watsona molecularanalysisoftheinteractionofthesnakevenomrhodocytinwiththeplateletreceptorclec2 AT ocallaghanc molecularanalysisoftheinteractionofthesnakevenomrhodocytinwiththeplateletreceptorclec2 |