2n27 | pdb_00002n27

Competitive inhibition of TRPV1 calmodulin interaction by vanilloids

spinqualitylabelsall models 2n27, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2n27 is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 4DY, CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 behaviour of these important pharmacons. This article is protected by copyright. All rights reserved. Competitive inhibition of TRPV1 - calmodulin interaction by vanilloids.,Hetenyi A, Nemeth L, Weber E, Szakonyi G, Winter Z, Josvay K, Bartus E, Olah Z, Martinek TA FEBS Lett. 2016 Jun 24. doi: 10.1002/1873-3468.12267. PMID:27339229 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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