4l76

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'''Unreleased structure'''
 
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The entry 4l76 is ON HOLD
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==Ca2+-bound E212Q mutant MthK RCK domain==
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<StructureSection load='4l76' size='340' side='right'caption='[[4l76]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4l76]] 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=4L76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L76 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.992&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4l76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l76 OCA], [https://pdbe.org/4l76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l76 RCSB], [https://www.ebi.ac.uk/pdbsum/4l76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l76 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MTHK_METTH MTHK_METTH] Calcium-gated potassium channel.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Smith, F.J., Rothberg, B.S.
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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>
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Description: Ca2+-bound E212Q mutant MthK RCK domain
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4l76" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Potassium channel 3D structures|Potassium channel 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Methanothermobacter thermautotrophicus str. Delta H]]
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[[Category: Rothberg BS]]
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[[Category: Smith FJ]]

Current revision

Ca2+-bound E212Q mutant MthK RCK domain

PDB ID 4l76

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