1vp6

From Proteopedia

(Difference between revisions)

Current revision

M.loti ion channel cylic nucleotide binding domain

Structural highlights

1vp6 is a 2 chain structure with sequence from Mesorhizobium loti. This structure supersedes the now removed PDB entry 1pf0. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.7Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vp6"

@@ Line 3: / Line 3: @@
 <StructureSection load='1vp6' size='340' side='right'caption='[[1vp6]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1vp6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700743 Atcc 700743]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1pf0 1pf0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VP6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VP6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1vp6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesorhizobium_loti Mesorhizobium loti]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1pf0 1pf0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VP6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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=1vp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vp6 OCA], [http://pdbe.org/1vp6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vp6 RCSB], [http://www.ebi.ac.uk/pdbsum/1vp6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vp6 ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vp6 OCA], [https://pdbe.org/1vp6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vp6 RCSB], [https://www.ebi.ac.uk/pdbsum/1vp6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vp6 ProSAT]</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>
+[https://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 36: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 700743]]
 [[Category: Large Structures]]
-[[Category: Clayton, G M]]
+[[Category: Mesorhizobium loti]]
-[[Category: Heginbotham, L]]
+[[Category: Clayton GM]]
-[[Category: Morais-Cabral, J H]]
+[[Category: Heginbotham L]]
-[[Category: Silverman, W R]]
+[[Category: Morais-Cabral JH]]
-[[Category: Dimer helical bundle beta barrel core with cyclic amp bound]]
+[[Category: Silverman WR]]
-[[Category: Membrane protein]]

1vp6

From Proteopedia

Current revision

M.loti ion channel cylic nucleotide binding domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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