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Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution fr...

Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution fr...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_fao_agris_US201600192550

Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel

About this item

Full title

Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2011-04, Vol.108 (15), p.6121-6126

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Cyclic nucleotide-sensitive ion channels, known as HCN and CNG channels, are activated by binding of ligands to a domain (CNBD) located on the cytoplasmic side of the channel. The underlying mechanisms are not well understood. To elucidate the gating mechanism, structures of both the ligand-free and -bound CNBD are required. Several crystal structu...

Alternative Titles

Full title

Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_fao_agris_US201600192550

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_fao_agris_US201600192550

Other Identifiers

ISSN

0027-8424,1091-6490

E-ISSN

1091-6490

DOI

10.1073/pnas.1015890108

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