期刊
PROTEIN & CELL
卷 8, 期 3, 页码 169-177出版社
HIGHER EDUCATION PRESS
DOI: 10.1007/s13238-016-0353-7
关键词
capsaicin; TRPV1; ligand gating; cryo-EM; computation; spiciness
类别
资金
- National Institutes of Health [R01NS072377]
- American Heart Association [14POST19820027]
Capsaicin in chili peppers bestows the sensation of spiciness. Since the discovery of its receptor, transient receptor potential vanilloid 1 (TRPV1) ion channel, how capsaicin activates this channel has been under extensive investigation using a variety of experimental techniques including mutagenesis, patch-clamp recording, crystallography, cryo-electron microscopy, computational docking and molecular dynamic simulation. A framework of how capsaicin binds and activates TRPV1 has started to merge: capsaicin binds to a pocket formed by the channel's transmembrane segments, where it takes a tail-up, head-down configuration. Binding is mediated by both hydrogen bonds and van der Waals interactions. Upon binding, capsaicin stabilizes the open state of TRPV1 by pull-and-contact with the S4-S5 linker. Understanding the ligand-host interaction will greatly facilitate pharmaceutical efforts to develop novel analgesics targeting TRPV1.
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