2N27
Competitive inhibition of TRPV1 calmodulin interaction by vanilloids
Summary for 2N27
| Entry DOI | 10.2210/pdb2n27/pdb |
| NMR Information | BMRB: 25588 |
| Descriptor | Calmodulin, CALCIUM ION, (6E)-N-(4-hydroxy-3-methoxybenzyl)-8-methylnon-6-enamide (3 entities in total) |
| Functional Keywords | calmodulin, capsaicin, metal binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm, cytoskeleton, spindle : P62158 |
| Total number of polymer chains | 1 |
| Total formula weight | 17187.07 |
| Authors | Hetenyi, A.,Nemeth, L.,Weber, E.,Szakonyi, G.,Winter, Z.,Josvay, K.,Bartus, E.,Olah, Z.,Martinek, T.A. (deposition date: 2015-04-29, release date: 2016-07-06, Last modification date: 2024-05-15) |
| Primary citation | Hetenyi, A.,Nemeth, L.,Weber, E.,Szakonyi, G.,Winter, Z.,Josvay, K.,Bartus, E.,Olah, Z.,Martinek, T.A. Competitive inhibition of TRPV1-calmodulin interaction by vanilloids. Febs Lett., 590:2768-2775, 2016 Cited by PubMed Abstract: There is enormous interest toward vanilloid agonists of the pain receptor TRPV1 in analgesic therapy, but the mechanisms of their sensory neuron-blocking effects at high or repeated doses are still a matter of debate. Our results have demonstrated that capsaicin and resiniferatoxin form nanomolar complexes with calmodulin, and competitively inhibit TRPV1-calmodulin interaction. These interactions involve the protein recognition interface of calmodulin, which is responsible for all of the cell-regulatory calmodulin-protein interactions. These results draw attention to a previously unknown vanilloid target, which may contribute to the explanation of the paradoxical pain-modulating behavior of these important pharmacons. PubMed: 27339229DOI: 10.1002/1873-3468.12267 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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