1u12

From Proteopedia

(Difference between revisions)

Revision as of 02:18, 11 September 2015

M. loti cyclic nucleotide binding domain mutant

Structural highlights

1u12 is a 2 chain structure with sequence from Mesorhizobium loti. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1pf0
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CNGK1_RHILO] Cyclic nucleotide-regulated potassium channel activated by cAMP.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Clayton GM, Silverman WR, Heginbotham L, Morais-Cabral JH. Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel. Cell. 2004 Nov 24;119(5):615-27. PMID:15550244 doi:10.1016/j.cell.2004.10.030
↑ Clayton GM, Silverman WR, Heginbotham L, Morais-Cabral JH. Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel. Cell. 2004 Nov 24;119(5):615-27. PMID:15550244 doi:10.1016/j.cell.2004.10.030

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u12"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pf0|1pf0]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u12 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1u12 RCSB], [http://www.ebi.ac.uk/pdbsum/1u12 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u12 OCA], [http://pdbe.org/1u12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u12 RCSB], [http://www.ebi.ac.uk/pdbsum/1u12 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CNGK1_RHILO CNGK1_RHILO]] Cyclic nucleotide-regulated potassium channel activated by cAMP.<ref>PMID:15550244</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1u12" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1u12

From Proteopedia

Revision as of 02:18, 11 September 2015

M. loti cyclic nucleotide binding domain mutant

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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