5FEB
Crystal structure of the Voltage-gated Sodium Channel Beta 2 subunit extracellular domain
Summary for 5FEB
| Entry DOI | 10.2210/pdb5feb/pdb |
| Related | 5FDY |
| Descriptor | Sodium channel subunit beta-2, GLYCEROL (3 entities in total) |
| Functional Keywords | membrane protein ion channel sodium, membrane protein |
| Biological source | Homo sapiens (Human) |
| Cellular location | Membrane; Single-pass type I membrane protein: O60939 |
| Total number of polymer chains | 1 |
| Total formula weight | 14653.57 |
| Authors | Das, S.,Van Petegem, F. (deposition date: 2015-12-16, release date: 2016-03-09, Last modification date: 2024-10-09) |
| Primary citation | Das, S.,Gilchrist, J.,Bosmans, F.,Van Petegem, F. Binary architecture of the Nav1.2-beta 2 signaling complex. Elife, 5:-, 2016 Cited by PubMed Abstract: To investigate the mechanisms by which β-subunits influence Nav channel function, we solved the crystal structure of the β2 extracellular domain at 1.35Å. We combined these data with known bacterial Nav channel structural insights and novel functional studies to determine the interactions of specific residues in β2 with Nav1.2. We identified a flexible loop formed by (72)Cys and (75)Cys, a unique feature among the four β-subunit isoforms. Moreover, we found that (55)Cys helps to determine the influence of β2 on Nav1.2 toxin susceptibility. Further mutagenesis combined with the use of spider toxins reveals that (55)Cys forms a disulfide bond with (910)Cys in the Nav1.2 domain II pore loop, thereby suggesting a 1:1 stoichiometry. Our results also provide clues as to which disulfide bonds are formed between adjacent Nav1.2 (912/918)Cys residues. The concepts emerging from this work will help to form a model reflecting the β-subunit location in a Nav channel complex. PubMed: 26894959DOI: 10.7554/eLife.10960 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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