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Keywords: nucleotide-binding domain
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Articles

Control of the CFTR channel's gates

P. Vergani, C. Basso, M. Mense, A.C. Nairn, D.C. Gadsby
Journal: Biochemical Society Transactions
Biochem Soc Trans (2005) 33 (5): 1003–1007.
DOI: https://doi.org/10.1042/BST0331003
Published: 26 October 2005
... and closing of its anion-selective pore are linked to ATP binding and hydrolysis at CFTR's two NBDs (nucleotide-binding domains), NBD1 and NBD2. Isolated NBDs of prokaryotic ABC proteins form homodimers upon binding ATP, but separate after hydrolysis of the ATP. By combining mutagenesis with single-channel...
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Articles

A molecular understanding of the catalytic cycle of the nucleotide-binding domain of the ABC transporter HlyB

J. Zaitseva, S. Jenewein, C. Oswald, T. Jumpertz, I.B. Holland, L. Schmitt
Journal: Biochemical Society Transactions
Biochem Soc Trans (2005) 33 (5): 990–995.
DOI: https://doi.org/10.1042/BST0330990
Published: 26 October 2005
... of the underlying transport mechanism remain an enigma. Similar to all other ABC transporters, ranging from bacteria to man, HlyB is composed of two NBDs (nucleotide-binding domains) and two transmembrane domains. Here we summarize our detailed biochemical, biophysical and structural studies aimed...
View article titled, A molecular understanding of the catalytic cycle of the <span class="search-highlight">nucleotide</span>-<span class="search-highlight">binding</span> <span class="search-highlight">domain</span> of the ABC transporter HlyB
Click here to open pdf in another window PDF for A molecular understanding of the catalytic cycle of the <span class="search-highlight">nucleotide</span>-<span class="search-highlight">binding</span> <span class="search-highlight">domain</span> of the ABC transporter HlyB
Articles

Structure-function relationships in the β -cell K ATP channel

M. V. Mikhailov, E. A. Mikhailova, S. J. H. Ashcroft
Journal: Biochemical Society Transactions
Biochem Soc Trans (2002) 30 (2): 323–327.
DOI: https://doi.org/10.1042/bst0300323
Published: 01 April 2002
... to the N-terminus of Kir6.2; (ii) the two nucleotide binding domains (NBDs) of SUR1 -NBD1 and NBD2 - are in proximity; (iii) transmembrane helix 12 of SUR1 is orientated in such a way that it can make contact with Kir6.2; (iv) formation of the glibenclamide binding site requires that the two cytosolic...
View article titled, Structure-function relationships in the β -cell K ATP channel
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