4l75: Difference between revisions
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== | ==Ca2+-bound D184N mutant MthK RCK domain at 2.4 Angstrom== | ||
[[http://www.uniprot.org/uniprot/MTHK_METTH MTHK_METTH | <StructureSection load='4l75' size='340' side='right'caption='[[4l75]], [[Resolution|resolution]] 2.39Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4l75]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus_str._Delta_H Methanothermobacter thermautotrophicus str. Delta H]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L75 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.393Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=4l75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l75 OCA], [https://pdbe.org/4l75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l75 RCSB], [https://www.ebi.ac.uk/pdbsum/4l75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l75 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://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> | ||
[[ | <div class="pdbe-citations 4l75" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Potassium channel 3D structures|Potassium channel 3D structures]] | |||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Methanothermobacter thermautotrophicus str. Delta H]] | |||
[[Category: Rothberg BS]] | |||
[[Category: Smith FJ]] |