Mccleverty, Clare, Koesema, Eric, Patapoutian, Ardem, Lesley, Scott and Kreusch, Andreas (2006) Crystal structure of the human TRPV2 channel ankyrin repeat domain. Protein Science : a publication of the Protein Society, 15 (9). pp. 2201-2206. ISSN 0961-8368

Abstract

TRPV channels are important polymodal integrators of noxious stimuli mediating thermosensation and nociception. An ankyrin repeat domain (ARD), which is a common protein-protein recognition domain, is conserved in the N-terminal intracellular domain of all TRPV channels and predicted to contain three to four ankyrin repeats. Here we report the first structure from the TRPV channel subfamily, a 1.7 A resolution crystal structure of the human TRPV2 ARD. Our crystal structure reveals a six ankyrin repeat stack with multiple insertions in each repeat generating several unique features compared with a canonical ARD. The surface typically used for ligand recognition, the ankyrin groove, contains extended loops with an exposed hydrophobic patch and a prominent kink resulting from a large rotational shift of the last two repeats. The TRPV2 ARD provides the first structural insight into a domain that coordinates nociceptive sensory transduction and is likely to be a prototype for other TRPV channel ARDs.

Item Type:	Article
Related URLs:	http://www.ncbi.nlm.nih.gov/sites/entrez... http://www.pubmedcentral.nih.gov/article...
Additional Information:	free final full text version available at publisher's official URL and at PubMedCentral; archiving not formally supported by this publisher
Keywords:	TRPV channel, ankyrin repeat, crystal structure
Related URLs:	http://www.ncbi.nlm.nih.gov/sites/entrez... http://www.pubmedcentral.nih.gov/article...
Date Deposited:	14 Dec 2009 14:04
Last Modified:	31 Jan 2013 01:26
URI:	https://oak.novartis.com/id/eprint/141