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Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating

Abstract:

KirBac channels are prokaryotic homologs of mammalian inwardly rectifying (Kir) potassium channels, and recent crystal structures of both Kir and KirBac channels have provided major insight into their unique structural architecture. However, all of the available structures are closed at the helix bundle crossing, and therefore the structural mechanisms that control opening of their primary activation gate remain unknown. In this study, we engineered the inner pore-lining helix (TM2) of KirBac...

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Publisher copy:
10.1038/nsmb.2208

Authors


Journal:
Nature Structural and Molecular Biology More from this journal
Volume:
19
Issue:
2
Pages:
158-164
Publication date:
2012-02-01
DOI:
EISSN:
1545-9985
ISSN:
1545-9993
Language:
English
Pubs id:
pubs:313995
UUID:
uuid:692713ea-b523-44eb-b8e8-92d14e26ec25
Local pid:
pubs:313995
Source identifiers:
313995
Deposit date:
2012-12-19

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