2M7Z
Structure of SmTSP2EC2
Summary for 2M7Z
| Entry DOI | 10.2210/pdb2m7z/pdb |
| NMR Information | BMRB: 19217 |
| Descriptor | CD63-like protein Sm-TSP-2 (1 entity in total) |
| Functional Keywords | tetraspanin, membrane protein, vaccine, schistosomasis |
| Biological source | Schistosoma mansoni (Blood fluke) |
| Cellular location | Membrane ; Multi-pass membrane protein : Q8ITD7 |
| Total number of polymer chains | 1 |
| Total formula weight | 9091.35 |
| Authors | Mulvenna, J.,Jia, X. (deposition date: 2013-05-02, release date: 2014-01-22, Last modification date: 2024-10-16) |
| Primary citation | Jia, X.,Schulte, L.,Loukas, A.,Pickering, D.,Pearson, M.,Mobli, M.,Jones, A.,Rosengren, K.J.,Daly, N.L.,Gobert, G.N.,Jones, M.K.,Craik, D.J.,Mulvenna, J. Solution structure, membrane interactions, and protein binding partners of the tetraspanin Sm-TSP-2, a vaccine antigen from the human blood fluke Schistosoma mansoni J.Biol.Chem., 289:7151-7163, 2014 Cited by PubMed Abstract: The tetraspanins (TSPs) are a family of integral membrane proteins that are ubiquitously expressed at the surface of eukaryotic cells. TSPs mediate a range of processes at the surface of the plasma membrane by providing a scaffold for the assembly of protein complexes known as tetraspanin-enriched microdomains (TEMs). We report here the structure of the surface-exposed EC2 domain from Sm-TSP-2, a TSP from Schistosoma mansoni and one of the better prospects for the development of a vaccine against schistosomiasis. This is the first solution structure of this domain, and our investigations of its interactions with lipid micelles provide a general model for interactions between TSPs, membranes, and other proteins. Using chemical cross-linking, eight potential protein constituents of Sm-TSP-2-mediated TEMs were also identified. These include proteins important for membrane maintenance and repair, providing further evidence for the functional role of Sm-TSP-2- and Sm-TSP-2-mediated TEMs. The identification of calpain, Sm29, and fructose-bisphosphate aldolase, themselves potential vaccine antigens, suggests that the Sm-TSP-2-mediated TEMs could be disrupted via multiple targets. The identification of further Sm-TSP-2-mediated TEM proteins increases the available candidates for multiplex vaccines and/or novel drugs targeting TEMs in the schistosome tegument. PubMed: 24429291DOI: 10.1074/jbc.M113.531558 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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