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Journal article

Non-equivalent role of TM2 gating hinges in heteromeric Kir4.1/Kir5.1 potassium channels.

Abstract:

Comparison of the crystal structures of the KcsA and MthK potassium channels suggests that the process of opening a K(+) channel involves pivoted bending of the inner pore-lining helices at a highly conserved glycine residue. This bending motion is proposed to splay the transmembrane domains outwards to widen the gate at the "helix-bundle crossing". However, in the inwardly rectifying (Kir) potassium channel family, the role of this "hinge" residue in the second transmembrane domain (TM2) and...

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Publication status:
Published

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Publisher copy:
10.1007/s00249-007-0206-7

Authors


More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Physics
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Physics
Sub department:
Condensed Matter Physics
Role:
Author
Journal:
European biophysics journal : EBJ
Volume:
37
Issue:
2
Pages:
165-171
Publication date:
2008-02-01
DOI:
EISSN:
1432-1017
ISSN:
0175-7571
Source identifiers:
24688

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