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PROTEIN STRUCTURE REPORT

Crystal structure of the human TRPV2 channel ankyrin repeat domain

¹ Genomics Institute of the Novartis Research Foundation, San Diego, California, 92121, USA
² Department of Cell Biology, The Scripps Research Institute, La Jolla, California, 92037, USA

(RECEIVED May 22, 2006; FINAL REVISION June 8, 2006; ACCEPTED June 9, 2006)

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 Å 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.

Keywords: TRPV channel; ankyrin repeat; crystal structure

Reprint requests to: Andreas Kreusch, Genomics Institute of the Novartis Research Foundation, 10675 John Jay Hopkins Drive, San Diego, CA 92121; e-mail: kreusch{at}gnf.org; fax: (858) 812-1746.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.062357206.

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