2m0q: Difference between revisions
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''' | ==Solution NMR analysis of intact KCNE2 in detergent micelles demonstrate a straight transmembrane helix== | ||
<StructureSection load='2m0q' size='340' side='right' caption='[[2m0q]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | |||
The entry | == Structural highlights == | ||
[[2m0q]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M0Q OCA]. <br> | |||
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br> | |||
== Disease == | |||
[[http://www.uniprot.org/uniprot/KCNE2_HUMAN KCNE2_HUMAN]] Familial atrial fibrillation;Romano-Ward syndrome. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/KCNE2_HUMAN KCNE2_HUMAN]] Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Associated with KCNH2/HERG is proposed to form the rapidly activating component of the delayed rectifying potassium current in heart (IKr). May associate with KCNQ2 and/or KCNQ3 and modulate the native M-type current. May associate with KCNQ1/KVLTQ1 and elicit a voltage-independent current. May associate with HCN1 and HCN2 and increase potassium current. | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chen, L.]] | |||
[[Category: Lai, C.]] | |||
[[Category: Li, P.]] | |||
[[Category: Tian, C.]] | |||
[[Category: Wu, F.]] | |||
[[Category: Zhang, L.]] | |||
[[Category: Detergent micelle]] | |||
[[Category: Membrane protein]] | |||
[[Category: Transmembrane helix]] | |||
Revision as of 07:53, 30 April 2014
Solution NMR analysis of intact KCNE2 in detergent micelles demonstrate a straight transmembrane helix
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