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2ptm

From Proteopedia

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Current revision

Structure and rearrangements in the carboxy-terminal region of SpIH channels

Structural highlights

2ptm is a 1 chain structure with sequence from Strongylocentrotus purpuratus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.93Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

O76977_STRPU

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

Hyperpolarization-activated cyclic nucleotide-modulated (HCN) ion channels regulate the spontaneous firing activity and electrical excitability of many cardiac and neuronal cells. The modulation of HCN channel opening by the direct binding of cAMP underlies many physiological processes such as the autonomic regulation of the heart rate. Here we use a combination of X-ray crystallography and electrophysiology to study the allosteric mechanism for cAMP modulation of HCN channels. SpIH is an invertebrate HCN channel that is activated fully by cAMP, but only partially by cGMP. We exploited the partial agonist action of cGMP on SpIH to reveal the molecular mechanism for cGMP specificity of many cyclic nucleotide-regulated enzymes. Our results also elaborate a mechanism for the allosteric conformational change in the cyclic nucleotide-binding domain and a mechanism for partial agonist action. These mechanisms will likely extend to other cyclic nucleotide-regulated channels and enzymes as well.

Structure and rearrangements in the carboxy-terminal region of SpIH channels.,Flynn GE, Black KD, Islas LD, Sankaran B, Zagotta WN Structure. 2007 Jun;15(6):671-82. PMID:17562314^[1]

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

References

↑ Flynn GE, Black KD, Islas LD, Sankaran B, Zagotta WN. Structure and rearrangements in the carboxy-terminal region of SpIH channels. Structure. 2007 Jun;15(6):671-82. PMID:17562314 doi:S0969-2126(07)00175-X

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/2ptm"

@@ Line 3: / Line 3: @@
 <StructureSection load='2ptm' size='340' side='right'caption='[[2ptm]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ptm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Purple_sea_urchin Purple sea urchin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PTM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PTM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ptm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Strongylocentrotus_purpuratus Strongylocentrotus purpuratus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PTM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PTM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</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]] 1.93&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</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=2ptm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ptm OCA], [https://pdbe.org/2ptm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ptm RCSB], [https://www.ebi.ac.uk/pdbsum/2ptm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ptm ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/O76977_STRPU O76977_STRPU]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 37: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Purple sea urchin]]
+[[Category: Strongylocentrotus purpuratus]]
-[[Category: Black, K D]]
+[[Category: Black KD]]
-[[Category: Flynn, G E]]
+[[Category: Flynn GE]]
-[[Category: Islas, L D]]
+[[Category: Islas LD]]
-[[Category: Sankaran, B]]
+[[Category: Sankaran B]]
-[[Category: Zagotta, W N]]
+[[Category: Zagotta WN]]
-[[Category: C-linker]]
-[[Category: Camp]]
-[[Category: Cgmp]]
-[[Category: Cyclic nucleotide binding domain]]
-[[Category: Hcn]]
-[[Category: Ion channel]]
-[[Category: Sphcn1]]
-[[Category: Transport protein]]

2ptm

From Proteopedia

Current revision

Structure and rearrangements in the carboxy-terminal region of SpIH channels

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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