1u12
From Proteopedia
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[[Image:1u12.gif|left|200px]] | [[Image:1u12.gif|left|200px]] | ||
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'''M. loti cyclic nucleotide binding domain mutant''' | '''M. loti cyclic nucleotide binding domain mutant''' | ||
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[[Category: Morais-Cabral, J H.]] | [[Category: Morais-Cabral, J H.]] | ||
[[Category: Silverman, W R.]] | [[Category: Silverman, W R.]] | ||
- | [[Category: | + | [[Category: C-helix mutation]] |
- | [[Category: | + | [[Category: Mutant cyclic nucleotide binding domain]] |
- | [[Category: | + | [[Category: Unliganded]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:37:18 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 07:37, 3 May 2008
M. loti cyclic nucleotide binding domain mutant
Overview
Here we describe the initial functional characterization of a cyclic nucleotide regulated ion channel from the bacterium Mesorhizobium loti and present two structures of its cyclic nucleotide binding domain, with and without cAMP. The domains are organized as dimers with the interface formed by the linker regions that connect the nucleotide binding pocket to the pore domain. Together, structural and functional data suggest the domains form two dimers on the cytoplasmic face of the channel. We propose a model for gating in which ligand binding alters the structural relationship within a dimer, directly affecting the position of the adjacent transmembrane helices.
About this Structure
1U12 is a Single protein structure of sequence from Mesorhizobium loti maff303099. Full crystallographic information is available from OCA.
Reference
Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel., Clayton GM, Silverman WR, Heginbotham L, Morais-Cabral JH, Cell. 2004 Nov 24;119(5):615-27. PMID:15550244 Page seeded by OCA on Sat May 3 10:37:18 2008