|
|
| (One intermediate revision by the same user not shown) |
| Line 1: |
Line 1: |
|
| |
|
| ==Cyclic nucleotide binding-homology domain from mouse EAG1 potassium channel== | | ==Cyclic nucleotide binding-homology domain from mouse EAG1 potassium channel== |
| <StructureSection load='4f8a' size='340' side='right' caption='[[4f8a]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='4f8a' size='340' side='right'caption='[[4f8a]], [[Resolution|resolution]] 2.20Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4f8a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 LK3 transgenic mice])</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]] 2.2Å</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://pdbe.org/4f8a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f8a RCSB], [http://www.ebi.ac.uk/pdbsum/4f8a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f8a ProSAT]</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> | | </table> |
| == Function == | | == Function == |
| [[http://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). | | [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). |
| <div style="background-color:#fffaf0;">
| |
| == Publication Abstract from PubMed ==
| |
| 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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| |
| </div>
| |
| <div class="pdbe-citations 4f8a" style="background-color:#fffaf0;"></div>
| |
| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Lk3 transgenic mice]] | | [[Category: Large Structures]] |
| [[Category: Cadene, M]] | | [[Category: Mus musculus]] |
| [[Category: Gabant, G]] | | [[Category: Cadene M]] |
| [[Category: Marques-Carvalho, M J]] | | [[Category: Gabant G]] |
| [[Category: Morais-Cabral, J H]] | | [[Category: Marques-Carvalho MJ]] |
| [[Category: Muskett, F W]] | | [[Category: Morais-Cabral JH]] |
| [[Category: Sahoo, N]] | | [[Category: Muskett FW]] |
| [[Category: Schonherr, R]] | | [[Category: Sahoo N]] |
| [[Category: Vieira-Pires, R S]] | | [[Category: Schonherr R]] |
| [[Category: Membrane protein]]
| | [[Category: Vieira-Pires RS]] |
| [[Category: Probable regulatory domain of potassium channel]]
| |
| [[Category: Transport protein]]
| |
