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2atk
From Proteopedia
| 2atk, resolution 2.50Å () | |||||||||
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| Sites: | , , , , , and | ||||||||
| Ligands: | , | ||||||||
| Related: | 1zwi | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Structure of a mutant KcsA K+ channel
We show that in the potassium channel KcsA, proton-dependent activation is followed by an inactivation process similar to C-type inactivation, and this process is suppressed by an E71A mutation in the pore helix. EPR spectroscopy demonstrates that the inner gate opens maximally at low pH regardless of the magnitude of the single-channel-open probability, implying that stationary gating originates mostly from rearrangements at the selectivity filter. Two E71A crystal structures obtained at 2.5 A reveal large structural excursions of the selectivity filter during ion conduction and provide a glimpse of the range of conformations available to this region of the channel during gating. These data establish a mechanistic basis for the role of the selectivity filter during channel activation and inactivation.
Molecular determinants of gating at the potassium-channel selectivity filter., Cordero-Morales JF, Cuello LG, Zhao Y, Jogini V, Cortes DM, Roux B, Perozo E, Nat Struct Mol Biol. 2006 Apr;13(4):311-8. Epub 2006 Mar 12. PMID:16532009
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2atk is a 3 chain structure of Monoclonal Antibody and Potassium Channel with sequence from Mus musculus and Streptomyces lividans. Full crystallographic information is available from OCA.
See Also
Reference
- Cordero-Morales JF, Cuello LG, Zhao Y, Jogini V, Cortes DM, Roux B, Perozo E. Molecular determinants of gating at the potassium-channel selectivity filter. Nat Struct Mol Biol. 2006 Apr;13(4):311-8. Epub 2006 Mar 12. PMID:16532009 doi:10.1038/nsmb1069
