Dijing Shi et al from KeWei Wang laboratory, in collaboration with Sheng Ye from Rongguang Zhang laboratory at the Institute of Biophysics, reported the crystal structure of TRPV3-ARD solved at 1.95 Å resolution published in the journal of PROTEIN AND CELL. TRPV3 plays critical roles in skin physiology and pathology, and TRPV3 is a multimodal cation channel that can be activated by temperature, natural compounds, endogenous ligands, synthetic small molecular 2-APB etc.

The structural analysis of TRPV3-ARD reveals the six-ankyrin repeats with longest finger 3 loop, distinct to known ARDs from other TRPV channels. The finger 3 of TRPV3-ARD bends over and forms extensive interactions with the repeats 3 and 4, representing a unique conformation that was not observed before. Patch clamp recordings of TRPV3 confirmed the role of TRPV3-ARD with characteristic finger 3 in channel function and pharmacology.

Shi DJ, Ye S, Cao X, Zhang R, Wang K. (2013) Crystal structure of the N-terminal ankyrin repeat domain of TRPV3 reveals unique conformation of finger 3 loop critical for channel function. Protein Cell . 2013 Dec;4(12):942-50.