2N27

Competitive inhibition of TRPV1 calmodulin interaction by vanilloids

2N27 の概要

• エントリーDOI: 10.2210/pdb2n27/pdb
• NMR情報: BMRB: 25588
• 分子名称: Calmodulin, CALCIUM ION, (6E)-N-(4-hydroxy-3-methoxybenzyl)-8-methylnon-6-enamide (3 entities in total)
• 機能のキーワード: calmodulin, capsaicin, metal binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytoskeleton, spindle : P62158
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17187.07

構造登録者

Hetenyi, A.,Nemeth, L.,Weber, E.,Szakonyi, G.,Winter, Z.,Josvay, K.,Bartus, E.,Olah, Z.,Martinek, T.A. (登録日: 2015-04-29, 公開日: 2016-07-06, 最終更新日: 2024-05-15)

主引用文献

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

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: 27339229
DOI: 10.1002/1873-3468.12267

実験手法

SOLUTION NMR