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4l76
From Proteopedia
(Difference between revisions)
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| - | + | ==Ca2+-bound E212Q mutant MthK RCK domain== | |
| - | + | <StructureSection load='4l76' size='340' side='right' caption='[[4l76]], [[Resolution|resolution]] 2.99Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4l76]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Metth Metth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L76 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L76 FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l73|4l73]], [[4l74|4l74]], [[4l75|4l75]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mthK, MTH_1520 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=187420 METTH])</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=4l76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l76 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l76 RCSB], [http://www.ebi.ac.uk/pdbsum/4l76 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/MTHK_METTH MTHK_METTH]] Calcium-gated potassium channel. | [[http://www.uniprot.org/uniprot/MTHK_METTH MTHK_METTH]] Calcium-gated potassium channel. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ligand binding sites within proteins can interact by allosteric mechanisms to modulate binding affinities and control protein function. Here we present crystal structures of the regulator of K(+) conductance (RCK) domain from a K(+) channel, MthK, which reveal the structural basis of allosteric coupling between two Ca(2+) regulatory sites within the domain. Comparison of RCK domain crystal structures in a range of conformations and with different numbers of regulatory Ca(2+) ions bound, combined with complementary electrophysiological analysis of channel gating, suggests chemical interactions that are important for modulation of ligand binding and subsequent channel opening. | ||
| + | |||
| + | Structural basis of allosteric interactions among Ca(2+)-binding sites in a K(+) channel RCK domain.,Smith FJ, Pau VP, Cingolani G, Rothberg BS Nat Commun. 2013;4:2621. doi: 10.1038/ncomms3621. PMID:24126388<ref>PMID:24126388</ref> | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | ==See Also== |
| - | + | *[[Potassium Channel|Potassium Channel]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Metth]] | [[Category: Metth]] | ||
| - | [[Category: Rothberg, B S | + | [[Category: Rothberg, B S]] |
| - | [[Category: Smith, F J | + | [[Category: Smith, F J]] |
[[Category: Calcium binding]] | [[Category: Calcium binding]] | ||
[[Category: Membrane-associated]] | [[Category: Membrane-associated]] | ||
Revision as of 08:47, 25 December 2014
Ca2+-bound E212Q mutant MthK RCK domain
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