4GIF
C-terminal coiled-coil domain of transient receptor potential channel TRPP3 (PKD2L1, Polycystin-L)
Summary for 4GIF
| Entry DOI | 10.2210/pdb4gif/pdb |
| Descriptor | Polycystic kidney disease 2-like 1 protein (2 entities in total) |
| Functional Keywords | coiled-coil, trimer, trp channel, transient receptor potential channel, polycystic kidney disease (pkd), membrane, transport protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Multi-pass membrane protein (Potential): Q9P0L9 |
| Total number of polymer chains | 1 |
| Total formula weight | 5102.93 |
| Authors | Yu, Y.,Ulbrich, M.H.,Li, M.-H.,Dobbins, S.,Zhang, W.K.,Tong, L.,Isacoff, E.Y.,Yang, J. (deposition date: 2012-08-08, release date: 2012-12-05, Last modification date: 2024-02-28) |
| Primary citation | Yu, Y.,Ulbrich, M.H.,Li, M.H.,Dobbins, S.,Zhang, W.K.,Tong, L.,Isacoff, E.Y.,Yang, J. Molecular mechanism of the assembly of an acid-sensing receptor ion channel complex. Nat Commun, 3:1252-1252, 2012 Cited by PubMed Abstract: Polycystic kidney disease (PKD) family proteins associate with transient receptor potential (TRP) channel family proteins to form functionally important complexes. PKD proteins differ from known ion channel-forming proteins and are generally thought to act as membrane receptors. Here we find that PKD1L3, a PKD protein, functions as a channel-forming subunit in an acid-sensing heteromeric complex formed by PKD1L3 and TRPP3, a TRP channel protein. Single amino-acid mutations in the putative pore region of both proteins alter the channel's ion selectivity. The PKD1L3/TRPP3 complex in the plasma membrane of live cells contains one PKD1L3 and three TRPP3. A TRPP3 C-terminal coiled-coil domain forms a trimer in solution and in crystal, and has a crucial role in the assembly and surface expression of the PKD1L3/TRPP3 complex. These results demonstrate that PKD subunits constitute a new class of channel-forming proteins, enriching our understanding of the function of PKD proteins and PKD/TRPP complexes. PubMed: 23212381DOI: 10.1038/ncomms2257 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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