3HRN
crystal structure of a C-terminal coiled coil domain of Transient receptor potential (TRP) channel subfamily P member 2 (TRPP2, polycystic kidney disease 2)
Summary for 3HRN
| Entry DOI | 10.2210/pdb3hrn/pdb |
| Related | 3HRO |
| Descriptor | Transient receptor potential (TRP) channel subfamily P member 2 (TRPP2) (2 entities in total) |
| Functional Keywords | coiled coil, helix bundle, trimer, calcium, disease mutation, glycoprotein, ion transport, ionic channel, membrane, phosphoprotein, polymorphism, transmembrane, transport, transport protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell projection, cilium membrane ; Multi-pass membrane protein : Q13563 |
| Total number of polymer chains | 1 |
| Total formula weight | 7352.63 |
| Authors | Yu, Y.,Ulbrich, M.H.,Li, M.-H.,Buraei, Z.,Chen, X.-Z.,Ong, A.C.M.,Tong, L.,Isacoff, E.Y.,Yang, J. (deposition date: 2009-06-09, release date: 2009-07-28, Last modification date: 2023-09-06) |
| Primary citation | Yu, Y.,Ulbrich, M.H.,Li, M.H.,Buraei, Z.,Chen, X.Z.,Ong, A.C.,Tong, L.,Isacoff, E.Y.,Yang, J. Structural and molecular basis of the assembly of the TRPP2/PKD1 complex. Proc.Natl.Acad.Sci.USA, 106:11558-11563, 2009 Cited by PubMed Abstract: Mutations in PKD1 and TRPP2 account for nearly all cases of autosomal dominant polycystic kidney disease (ADPKD). These 2 proteins form a receptor/ion channel complex on the cell surface. Using a combination of biochemistry, crystallography, and a single-molecule method to determine the subunit composition of proteins in the plasma membrane of live cells, we find that this complex contains 3 TRPP2 and 1 PKD1. A newly identified coiled-coil domain in the C terminus of TRPP2 is critical for the formation of this complex. This coiled-coil domain forms a homotrimer, in both solution and crystal structure, and binds to a single coiled-coil domain in the C terminus of PKD1. Mutations that disrupt the TRPP2 coiled-coil domain trimer abolish the assembly of both the full-length TRPP2 trimer and the TRPP2/PKD1 complex and diminish the surface expression of both proteins. These results have significant implications for the assembly, regulation, and function of the TRPP2/PKD1 complex and the pathogenic mechanism of some ADPKD-producing mutations. PubMed: 19556541DOI: 10.1073/pnas.0903684106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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