2F37

Crystal structure of the ankyrin repeat domain of human TRPV2

Summary for 2F37

• Entry DOI: 10.2210/pdb2f37/pdb
• Descriptor: Transient receptor potential cation channel subfamily V member 2, SULFATE ION (3 entities in total)
• Functional Keywords: ankyrin repeat, membrane protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Multi-pass membrane protein (By similarity): Q9Y5S1
• Total number of polymer chains: 2
• Total formula weight: 56014.63

Authors

McCleverty, C.J. (deposition date: 2005-11-18, release date: 2006-10-31, Last modification date: 2011-07-13)

Primary citation

McCleverty, C.J.,Koesema, E.,Patapoutian, A.,Lesley, S.A.,Kreusch, A.
Crystal structure of the human TRPV2 channel ankyrin repeat domain.
Protein Sci., 15:2201-2206, 2006

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.

PubMed: 16882997
DOI: 10.1110/ps.062357206

Experimental method

X-RAY DIFFRACTION (1.7 Å)