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4f8a

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Cyclic nucleotide binding-homology domain from mouse EAG1 potassium channel

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Retrieved from "http://52.214.119.220/wiki/index.php/4f8a"

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 ==Cyclic nucleotide binding-homology domain from mouse EAG1 potassium channel==
-<StructureSection load='4f8a' size='340' side='right' caption='[[4f8a]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='4f8a' size='340' side='right'caption='[[4f8a]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4f8a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F8A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F8A FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4f8a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F8A FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Eag, Kcnh1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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]] 2.2&#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=4f8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f8a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f8a RCSB], [http://www.ebi.ac.uk/pdbsum/4f8a PDBsum]</span></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=4f8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f8a OCA], [https://pdbe.org/4f8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f8a RCSB], [https://www.ebi.ac.uk/pdbsum/4f8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f8a ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/KCNH1_MOUSE KCNH1_MOUSE] Pore-forming (alpha) subunit of voltage-gated non-inactivating delayed rectifier potassium channel. Channel properties may be modulated by cAMP and subunit assembly. Mediates IK(NI) current in myoblasts (By similarity).
-KCNH channels are voltage-gated potassium channels with important physiological functions. In these channels, a C-terminal cytoplasmic region, known as the cyclic nucleotide binding homology (CNB-homology) domain displays strong sequence similarity to cyclic nucleotide binding (CNB) domains. However, the isolated domain does not bind cyclic nucleotides. Here, we report the X-ray structure of the CNB-homology domain from the mouse EAG1 channel. Through comparison with the recently determined structure of the CNB-homology domain from the zebrafish ELK (eag-like K(+)) channel and the CNB domains from the MlotiK1 and HCN (hyperpolarization-activated cyclic nucleotide-gated) potassium channels, we establish the structural features of CNB-homology domains that explain the low affinity for cyclic nucleotides. Our structure establishes that the "self-liganded" conformation, where two residues of the C-terminus of the domain are bound in an equivalent position to cyclic nucleotides in CNB domains, is a conserved feature of CNB-homology domains. Importantly, we provide biochemical evidence that suggests that there is also an unliganded conformation where the C-terminus of the domain peels away from its bound position. A functional characterization of this unliganded conformation reveals a role of the CNB-homology domain in channel gating.
-Structural, Biochemical, and Functional Characterization of the Cyclic Nucleotide Binding Homology Domain from the Mouse EAG1 Potassium Channel.,Marques-Carvalho MJ, Sahoo N, Muskett FW, Vieira-Pires RS, Gabant G, Cadene M, Schonherr R, Morais-Cabral JH J Mol Biol. 2012 Jun 23. PMID:22732247<ref>PMID:22732247</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Cadene, M]]
+[[Category: Cadene M]]
-[[Category: Gabant, G]]
+[[Category: Gabant G]]
-[[Category: Marques-Carvalho, M J]]
+[[Category: Marques-Carvalho MJ]]
-[[Category: Morais-Cabral, J H]]
+[[Category: Morais-Cabral JH]]
-[[Category: Muskett, F W]]
+[[Category: Muskett FW]]
-[[Category: Sahoo, N]]
+[[Category: Sahoo N]]
-[[Category: Schonherr, R]]
+[[Category: Schonherr R]]
-[[Category: Vieira-Pires, R S]]
+[[Category: Vieira-Pires RS]]
-[[Category: Membrane protein]]
-[[Category: Probable regulatory domain of potassium channel]]
-[[Category: Transport protein]]

4f8a

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Cyclic nucleotide binding-homology domain from mouse EAG1 potassium channel

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