4hoi: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of PAS domain from the mouse EAG1 potassium channel== | ==Crystal structure of PAS domain from the mouse EAG1 potassium channel== | ||
<StructureSection load='4hoi' size='340' side='right' caption='[[4hoi]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='4hoi' size='340' side='right' caption='[[4hoi]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4hoi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4hoi]] is a 4 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=4HOI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HOI FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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">[[1byw|1byw]], [[4hp4|4hp4]], [[4hp9|4hp9]], [[4hqa|4hqa]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1byw|1byw]], [[4hp4|4hp4]], [[4hp9|4hp9]], [[4hqa|4hqa]]</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 | <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> | ||
<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=4hoi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hoi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hoi RCSB], [http://www.ebi.ac.uk/pdbsum/4hoi 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=4hoi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hoi OCA], [http://pdbe.org/4hoi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hoi RCSB], [http://www.ebi.ac.uk/pdbsum/4hoi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hoi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 18: | Line 19: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4hoi" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
| Line 25: | Line 27: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Lk3 transgenic mice]] | ||
[[Category: Adaixo, R]] | [[Category: Adaixo, R]] | ||
[[Category: Morais-Cabral, J H]] | [[Category: Morais-Cabral, J H]] | ||
[[Category: Potassium channel domain]] | [[Category: Potassium channel domain]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
Revision as of 13:34, 4 August 2016
Crystal structure of PAS domain from the mouse EAG1 potassium channelCrystal structure of PAS domain from the mouse EAG1 potassium channel
Structural highlights
Function[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). Publication Abstract from PubMedKCNH channels form an important family of voltage gated potassium channels. These channels include a N-terminal Per-Arnt-Sim (PAS) domain with unknown function. In other proteins PAS domains are implicated in cellular responses to environmental queues through small molecule binding or involvement in signaling cascades. To better understand their role we characterized the structural properties of several channel PAS domains. We determined high resolution structures of PAS domains from the mouse EAG (mEAG), drosophila ELK (dELK) and human ERG (hERG) channels and also of the hERG domain without the first nine amino acids. We analyzed these structures for features connected to ligand binding and signaling in other PAS domains. In particular, we have found cavities in the hERG and mEAG structures that share similarities with the ligand binding sites from other PAS domains. These cavities are lined by polar and apolar chemical groups and display potential flexibility in their volume. We have also found that the hydrophobic patch on the domain beta-sheet is a conserved feature and appears to drive the formation of protein-protein contacts. In addition, the structures of the dELK domain and of the truncated hERG domain revealed the presence of N-terminal helices. These helices are equivalent to the helix described in the hERG NMR structures and are known to be important for channel function. Overall, these channel domains retain many of the PAS domain characteristics known to be important for cell signaling. Structural properties of PAS domains from the KCNH potassium channels.,Adaixo R, Harley CA, Castro-Rodrigues AF, Morais-Cabral JH PLoS One. 2013;8(3):e59265. doi: 10.1371/journal.pone.0059265. Epub 2013 Mar 15. PMID:23555008[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||