3SWF
CNGA1 621-690 containing CLZ domain
Summary for 3SWF
| Entry DOI | 10.2210/pdb3swf/pdb |
| Related | 3SWY |
| Descriptor | cGMP-gated cation channel alpha-1, ZINC ION (3 entities in total) |
| Functional Keywords | coiled-coil, assembly domain, transport protein |
| Biological source | Bos taurus (bovine) |
| Cellular location | Membrane; Multi-pass membrane protein: Q00194 |
| Total number of polymer chains | 3 |
| Total formula weight | 25049.92 |
| Authors | Shuart, N.G.,Haitin, Y.,Camp, S.S.,Black, K.D.,Zagotta, W.N. (deposition date: 2011-07-13, release date: 2011-09-14, Last modification date: 2023-09-13) |
| Primary citation | Shuart, N.G.,Haitin, Y.,Camp, S.S.,Black, K.D.,Zagotta, W.N. Molecular mechanism for 3:1 subunit stoichiometry of rod cyclic nucleotide-gated ion channels. Nat Commun, 2:457-457, 2011 Cited by PubMed Abstract: Molecular determinants of ion channel tetramerization are well characterized, but those involved in heteromeric channel assembly are less clearly understood. The heteromeric composition of native channels is often precisely controlled. Cyclic nucleotide-gated (CNG) channels from rod photoreceptors exhibit a 3:1 stoichiometry of CNGA1 and CNGB1 subunits that tunes the channels for their specialized role in phototransduction. Here we show, using electrophysiology, fluorescence, biochemistry, and X-ray crystallography, that the mechanism for this controlled assembly is the formation of a parallel 3-helix coiled-coil domain of the carboxy-terminal leucine zipper region of CNGA1 subunits, constraining the channel to contain three CNGA1 subunits, followed by preferential incorporation of a single CNGB1 subunit. Deletion of the carboxy-terminal leucine zipper domain relaxed the constraint and permitted multiple CNGB1 subunits in the channel. The X-ray crystal structures of the parallel 3-helix coiled-coil domains of CNGA1 and CNGA3 subunits were similar, suggesting that a similar mechanism controls the stoichiometry of cone CNG channels. PubMed: 21878911DOI: 10.1038/ncomms1466 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.14 Å) |
Structure validation
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