Crystal structure of the human TRPV2 channel ankyrin repeat domain.
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McCleverty CJ, Koesema E, Patapoutian A, Lesley SA, Kreusch A
Crystal structure of the human TRPV2 channel ankyrin repeat domain.
Protein Sci. 2006 Sep;15(9):2201-6. Epub 2006 Aug 1.
- PubMed ID
- 16882997 [ View in PubMed]
- 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.