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2atk

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{{STRUCTURE_2atk| PDB=2atk | SCENE= }}
{{STRUCTURE_2atk| PDB=2atk | SCENE= }}
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'''Structure of a mutant KcsA K+ channel'''
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===Structure of a mutant KcsA K+ channel===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_16532009}}
==About this Structure==
==About this Structure==
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[[Category: Mutant kcsa]]
[[Category: Mutant kcsa]]
[[Category: Protein-antibody fab complex]]
[[Category: Protein-antibody fab complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:27:42 2008''
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Revision as of 14:11, 28 July 2008

Image:2atk.png

Template:STRUCTURE 2atk

Structure of a mutant KcsA K+ channel

Template:ABSTRACT PUBMED 16532009

About this Structure

2ATK is a Single protein structure of sequence from Mus musculus and Streptomyces lividans. Full crystallographic information is available from OCA.

Reference

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

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