4l75: Difference between revisions
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==Ca2+-bound D184N mutant MthK RCK domain at 2.4 Angstrom== | |||
<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]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Methanothermobacter thermautotrophicus str. Delta H]] | |||
[[Category: Rothberg BS]] | |||
[[Category: Smith FJ]] | |||
Latest revision as of 19:13, 20 September 2023
Ca2+-bound D184N mutant MthK RCK domain at 2.4 AngstromCa2+-bound D184N mutant MthK RCK domain at 2.4 Angstrom
Structural highlights
FunctionMTHK_METTH Calcium-gated potassium channel. Publication Abstract from PubMedLigand 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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