1EOF
CRYSTAL STRUCTURE OF THE N136A MUTANT OF A SHAKER T1 DOMAIN
Summary for 1EOF
| Entry DOI | 10.2210/pdb1eof/pdb |
| Related | 1EOD 1EOE 1T1D |
| Descriptor | POTASSIUM CHANNEL KV1.1 (2 entities in total) |
| Functional Keywords | potassium channels, aplysia kv1.1, proton transport, membrane protein |
| Biological source | Aplysia californica (California sea hare) |
| Total number of polymer chains | 1 |
| Total formula weight | 12054.43 |
| Authors | Nanao, M.H.,Cushman, S.J.,Jahng, A.W.,DeRubeis, D.,Choe, S.,Pfaffinger, P.J. (deposition date: 2000-03-22, release date: 2000-05-02, Last modification date: 2024-02-07) |
| Primary citation | Cushman, S.J.,Nanao, M.H.,Jahng, A.W.,DeRubeis, D.,Choe, S.,Pfaffinger, P.J. Voltage dependent activation of potassium channels is coupled to T1 domain structure. Nat.Struct.Biol., 7:403-407, 2000 Cited by PubMed Abstract: The T1 domain, a highly conserved cytoplasmic portion at the N-terminus of the voltage-dependent K+ channel (Kv) alpha-subunit, is responsible for driving and regulating the tetramerization of the alpha-subunits. Here we report the identification of a set of mutations in the T1 domain that alter the gating properties of the Kv channel. Two mutants produce a leftward shift in the activation curve and slow the channel closing rate while a third mutation produces a rightward shift in the activation curve and speeds the channel closing rate. We have determined the crystal structures of T1 domains containing these mutations. Both of the leftward shifting mutants produce similar conformational changes in the putative membrane facing surface of the T1 domain. These results suggest that the structure of the T1 domain in this region is tightly coupled to the channel's gating states. PubMed: 10802739DOI: 10.1038/75185 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.38 Å) |
Structure validation
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