Molecular Structure of Transient Receptor Potential Vanilloid Type 1 Ion Channel (TRPV1)

Author(s): Laszlo Urban, John P.M. White, Istvan Nagy.

Journal Name: Current Pharmaceutical Biotechnology

Volume 12 , Issue 1 , 2011

Become EABM
Become Reviewer


Elaboration of the structure of TRPV1 and its functional relationship with channel activity is a work in progress, with much remaining to be done before the structure-function relationship of TRPV1 is comprehensively elicited. The result is that the present state of knowledge can reasonably be described as a patch-work of insightful data where major deficits in knowledge remain and where meaningful general conclusions cannot be reliably drawn. This is unfortunate, given that this ion channel has been convincingly implicated in a wide range of physiological functions and pathological conditions. Moreover, the development of therapeutic strategies which target TRPV1 depends on the knowledge of this receptors structure and its relationship with channel function. Here, we offer a description of the present state of knowledge in relation to this complex subject.

Keywords: TRPV1, structure, receptor, channel, pain, capsaicin, vanilloid sub-family, transducisomes, PKC, FAF1, synaptotagmin, TRPV1 signalling complex, NGF receptor, ankyrin repeat domains, ARDs, oligomerization, calmodulin, desensitisation, PIP2, TRP domain, TRP box, juxtamembrane, mutagenesis studies, tyrosine, RTX, noxious stimuli, TRPM8, phosphorylation, synergistic, stimulus integrator

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2011
Page: [115 - 121]
Pages: 7
DOI: 10.2174/138920111793937934

Article Metrics

PDF: 18