4l74: Difference between revisions
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==Ca2+-bound MthK RCK domain at 1.9 Angstrom with single ligand== | |||
<StructureSection load='4l74' size='340' side='right' caption='[[4l74]], [[Resolution|resolution]] 1.84Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4l74]] is a 2 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=4L74 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L74 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l73|4l73]], [[4l75|4l75]], [[4l76|4l76]]</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=4l74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l74 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l74 RCSB], [http://www.ebi.ac.uk/pdbsum/4l74 PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[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: Cingolani, G | [[Category: Cingolani, G]] | ||
[[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]] | ||