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
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Authors
Bibliographic Details
- 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
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:24688
- UUID:
-
uuid:3615ab5f-f28b-4f37-80db-f3ec436509da
- Local pid:
- pubs:24688
- Deposit date:
- 2012-12-19
Terms of use
- Copyright date:
- 2008
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