1vp6: Difference between revisions
New page: left|200px<br /><applet load="1vp6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vp6, resolution 1.70Å" /> '''M.loti ion channel c... |
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[[Image:1vp6.jpg|left|200px]]<br /><applet load="1vp6" size=" | [[Image:1vp6.jpg|left|200px]]<br /><applet load="1vp6" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1vp6, resolution 1.70Å" /> | caption="1vp6, resolution 1.70Å" /> | ||
'''M.loti ion channel cylic nucleotide binding domain'''<br /> | '''M.loti ion channel cylic nucleotide binding domain'''<br /> | ||
==Overview== | ==Overview== | ||
Here we describe the initial functional characterization of a cyclic | 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== | ==About this Structure== | ||
1VP6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mesorhizobium_loti Mesorhizobium loti] with BR and CMP as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | 1VP6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mesorhizobium_loti Mesorhizobium loti] with <scene name='pdbligand=BR:'>BR</scene> and <scene name='pdbligand=CMP:'>CMP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1PF0. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VP6 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Mesorhizobium loti]] | [[Category: Mesorhizobium loti]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Clayton, G | [[Category: Clayton, G M.]] | ||
[[Category: Heginbotham, L.]] | [[Category: Heginbotham, L.]] | ||
[[Category: Morais-Cabral, J | [[Category: Morais-Cabral, J H.]] | ||
[[Category: Silverman, W | [[Category: Silverman, W R.]] | ||
[[Category: BR]] | [[Category: BR]] | ||
[[Category: CMP]] | [[Category: CMP]] | ||
[[Category: dimer helical bundle beta barrel core with cyclic amp bound]] | [[Category: dimer helical bundle beta barrel core with cyclic amp bound]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:37:07 2008'' |
Revision as of 16:37, 21 February 2008
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M.loti ion channel cylic nucleotide binding domain
OverviewOverview
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 StructureAbout this Structure
1VP6 is a Single protein structure of sequence from Mesorhizobium loti with and as ligands. This structure supersedes the now removed PDB entry 1PF0. Full crystallographic information is available from OCA.
ReferenceReference
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
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