4l75: Difference between revisions

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{{STRUCTURE_4l75|  PDB=4l75  |  SCENE=  }}
==Ca2+-bound D184N mutant MthK RCK domain at 2.4 Angstrom==
===Ca2+-bound D184N mutant MthK RCK domain at 2.4 Angstrom===
<StructureSection load='4l75' size='340' side='right' caption='[[4l75]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
{{ABSTRACT_PUBMED_24126388}}
== Structural highlights ==
<table><tr><td colspan='2'>[[4l75]] 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=4L75 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L75 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]], [[4l74|4l74]], [[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=4l75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l75 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l75 RCSB], [http://www.ebi.ac.uk/pdbsum/4l75 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.


==Function==
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>
[[http://www.uniprot.org/uniprot/MTHK_METTH MTHK_METTH]] Calcium-gated potassium channel.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[4l75]] 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=4L75 OCA].
</div>


==Reference==
==See Also==
<ref group="xtra">PMID:024126388</ref><references group="xtra"/><references/>
*[[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 05:42, 25 December 2014

Ca2+-bound D184N mutant MthK RCK domain at 2.4 AngstromCa2+-bound D184N mutant MthK RCK domain at 2.4 Angstrom

Structural highlights

4l75 is a 6 chain structure with sequence from Metth. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:mthK, MTH_1520 (METTH)
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[MTHK_METTH] Calcium-gated potassium channel.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Smith FJ, Pau VP, Cingolani G, Rothberg BS. Structural basis of allosteric interactions among Ca(2+)-binding sites in a K(+) channel RCK domain. Nat Commun. 2013;4:2621. doi: 10.1038/ncomms3621. PMID:24126388 doi:http://dx.doi.org/10.1038/ncomms3621

4l75, resolution 2.39Å

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