This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2m0q
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | ''' | + | ==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=''> | |
| - | + | == 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
| |||||||||||
