2I2R
Crystal structure of the KChIP1/Kv4.3 T1 complex
Summary for 2I2R
| Entry DOI | 10.2210/pdb2i2r/pdb |
| Descriptor | Potassium voltage-gated channel subfamily D member 3, Kv channel-interacting protein 1, ZINC ION, ... (5 entities in total) |
| Functional Keywords | ef-hand protein, complex, potassium channel, ncs protein, calcium binding protein, transport protein |
| Biological source | Rattus norvegicus (Norway rat) More |
| Cellular location | Cell membrane; Multi-pass membrane protein: Q62897 Cell membrane; Peripheral membrane protein (By similarity): Q9NZI2 |
| Total number of polymer chains | 16 |
| Total formula weight | 303949.37 |
| Authors | Findeisen, F.,Pioletti, M.,Minor Jr., D.L. (deposition date: 2006-08-16, release date: 2006-10-24, Last modification date: 2023-08-30) |
| Primary citation | Pioletti, M.,Findeisen, F.,Hura, G.L.,Minor Jr., D.L. Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer Nat.Struct.Mol.Biol., 13:987-995, 2006 Cited by PubMed Abstract: Brain I(A) and cardiac I(to) currents arise from complexes containing Kv4 voltage-gated potassium channels and cytoplasmic calcium-sensor proteins (KChIPs). Here, we present X-ray crystallographic and small-angle X-ray scattering data that show that the KChIP1-Kv4.3 N-terminal cytoplasmic domain complex is a cross-shaped octamer bearing two principal interaction sites. Site 1 comprises interactions between a unique Kv4 channel N-terminal hydrophobic segment and a hydrophobic pocket formed by displacement of the KChIP H10 helix. Site 2 comprises interactions between a T1 assembly domain loop and the KChIP H2 helix. Functional and biochemical studies indicate that site 1 influences channel trafficking, whereas site 2 affects channel gating, and that calcium binding is intimately linked to KChIP folding and complex formation. Together, the data resolve how Kv4 channels and KChIPs interact and provide a framework for understanding how KChIPs modulate Kv4 function. PubMed: 17057713DOI: 10.1038/nsmb1164 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.35 Å) |
Structure validation
Download full validation report
