6CUD
Structure of the human TRPC3 in a lipid-occupied, closed state
Summary for 6CUD
| Entry DOI | 10.2210/pdb6cud/pdb |
| EMDB information | 7620 |
| Descriptor | Short transient receptor potential channel 3, (2S)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(hexanoyloxy)propyl hexanoate, (2R)-3-hydroxypropane-1,2-diyl dihexanoate, ... (4 entities in total) |
| Functional Keywords | canonical transient receptor potential 3 (trpc3) lipid-sensitive non-selective cation channel, membrane protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 374449.03 |
| Authors | |
| Primary citation | Fan, C.,Choi, W.,Sun, W.,Du, J.,Lu, W. Structure of the human lipid-gated cation channel TRPC3. Elife, 7:-, 2018 Cited by PubMed Abstract: The TRPC channels are crucially involved in store-operated calcium entry and calcium homeostasis, and they are implicated in human diseases such as neurodegenerative disease, cardiac hypertrophy, and spinocerebellar ataxia. We present a structure of the full-length human TRPC3, a lipid-gated TRPC member, in a lipid-occupied, closed state at 3.3 Angstrom. TRPC3 has four elbow-like membrane reentrant helices prior to the first transmembrane helix. The TRP helix is perpendicular to, and thus disengaged from, the pore-lining S6, suggesting a different gating mechanism from other TRP subfamily channels. The third transmembrane helix S3 is remarkably long, shaping a unique transmembrane domain, and constituting an extracellular domain that may serve as a sensor of external stimuli. We identified two lipid-binding sites, one being sandwiched between the pre-S1 elbow and the S4-S5 linker, and the other being close to the ion-conducting pore, where the conserved LWF motif of the TRPC family is located. PubMed: 29726814DOI: 10.7554/eLife.36852 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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