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

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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 receptor's structure and its relationship with channel function. Here, we offer a description of the present state of knowledge in relation to this complex subject.

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

Document Type: Research Article

Publication date: 01 January 2011

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  • Current Pharmaceutical Biotechnology aims to cover all the latest and outstanding developments in Pharmaceutical Biotechnology. Each issue of the journal contains a series of timely in-depth reviews written by leaders in the field covering a range of current topics in both pre-clinical and clinical areas of Pharmaceutical Biotechnology. Current Pharmaceutical Biotechnology is an essential journal for academic, clinical, government and pharmaceutical scientists who wish to be kept informed and up-to-date with the latest and most important developments.
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