4N5Q
Crystal structure of the N-terminal ankyrin repeat domain of TRPV3
Summary for 4N5Q
| Entry DOI | 10.2210/pdb4n5q/pdb |
| Descriptor | Transient receptor potential cation channel subfamily V member 3 (2 entities in total) |
| Functional Keywords | ankyrin, channel, protein binding |
| Biological source | Mus musculus (mouse) |
| Cellular location | Membrane; Multi-pass membrane protein (Probable): Q8K424 |
| Total number of polymer chains | 2 |
| Total formula weight | 58689.02 |
| Authors | Shi, D.J.,Ye, S.,Cao, X.,Wang, K.W.,Zhang, R. (deposition date: 2013-10-10, release date: 2014-01-29, Last modification date: 2024-03-20) |
| Primary citation | Shi, D.J.,Ye, S.,Cao, X.,Zhang, R.,Wang, K. Crystal structure of the N-terminal ankyrin repeat domain of TRPV3 reveals unique conformation of finger 3 loop critical for channel function Protein Cell, 4:942-950, 2013 Cited by PubMed Abstract: In all six members of TRPV channel subfamily, there is an ankyrin repeat domain (ARD) in their intracellular N-termini. Ankyrin (ANK) repeat, a common motif with typically 33 residues in each repeat, is primarily involved in protein-protein interactions. Despite the sequence similarity among the ARDs of TRPV channels, the structure of TRPV3-ARD, however, remains unknown. Here, we report the crystal structure of TRPV3-ARD solved at 1.95 Å resolution, which reveals six-ankyrin repeats. While overall structure of TRPV3-ARD is similar to ARDs from other members of TRPV subfamily; it, however, features a noticeable finger 3 loop that bends over and is stabilized by a network of hydrogen bonds and hydrophobic packing, instead of being flexible as seen in known TRPV-ARD structures. Electrophysiological recordings demonstrated that mutating key residues R225, R226, Q255, and F249 of finger 3 loop altered the channel activities and pharmacology. Taken all together, our findings show that TRPV3-ARD with characteristic finger 3 loop likely plays an important role in channel function and pharmacology. PubMed: 24248473DOI: 10.1007/s13238-013-3091-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.946 Å) |
Structure validation
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