1r10
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(New page: 200px<br /><applet load="1r10" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r10, resolution 3.00Å" /> '''Cystic fibrosis tran...)
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Revision as of 23:03, 20 November 2007
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Cystic fibrosis transmembrane conductance regulator (CFTR) nucleotide-binding domain one (NBD1) with ATP, I4122 space group
Overview
Cystic fibrosis transmembrane conductance regulator (CFTR) is an, ATP-binding cassette (ABC) transporter that functions as a chloride, channel. Nucleotide-binding domain 1 (NBD1), one of two ABC domains in, CFTR, also contains sites for the predominant CF-causing mutation and, potentially, for regulatory phosphorylation. We have determined crystal, structures for mouse NBD1 in unliganded, ADP- and ATP-bound states, with, and without phosphorylation. This NBD1 differs from typical ABC domains in, having added regulatory segments, a foreshortened subdomain, interconnection, and an unusual nucleotide conformation. Moreover, isolated NBD1 has undetectable ATPase activity and its structure is, essentially the same independent of ligand state. Phe508, which is, commonly deleted in CF, is exposed at a putative NBD1-transmembrane, interface. Our results are consistent with a CFTR mechanism, whereby, channel gating occurs through ATP binding in an NBD1-NBD2 nucleotide, sandwich that forms upon displacement of NBD1 regulatory segments.
About this Structure
1R10 is a Single protein structure of sequence from Mus musculus with MG, ATP and ACY as ligands. Full crystallographic information is available from OCA.
Reference
Structure of nucleotide-binding domain 1 of the cystic fibrosis transmembrane conductance regulator., Lewis HA, Buchanan SG, Burley SK, Conners K, Dickey M, Dorwart M, Fowler R, Gao X, Guggino WB, Hendrickson WA, Hunt JF, Kearins MC, Lorimer D, Maloney PC, Post KW, Rajashankar KR, Rutter ME, Sauder JM, Shriver S, Thibodeau PH, Thomas PJ, Zhang M, Zhao X, Emtage S, EMBO J. 2004 Jan 28;23(2):282-93. Epub 2003 Dec 18. PMID:14685259
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