4qfr
From Proteopedia
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qfr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qfr RCSB], [http://www.ebi.ac.uk/pdbsum/4qfr PDBsum]</span></td></tr> | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qfr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qfr RCSB], [http://www.ebi.ac.uk/pdbsum/4qfr PDBsum]</span></td></tr> | ||
<table> | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | AMP-activated protein kinase (AMPK) is a principal metabolic regulator affecting growth and response to cellular stress. Comprised of catalytic and regulatory subunits, each present in multiple forms, AMPK is best described as a family of related enzymes. In recent years, AMPK has emerged as a desirable target for modulation of numerous diseases, yet clinical therapies remain elusive. Challenges result, in part, from an incomplete understanding of the structure and function of full-length heterotrimeric complexes. In this work, we provide the full-length structure of the widely expressed alpha1beta1gamma1 isoform of mammalian AMPK, along with detailed kinetic and biophysical characterization. We characterize binding of the broadly studied synthetic activator A769662 and its analogs. Our studies follow on the heels of the recent disclosure of the alpha2beta1gamma1 structure and provide insight into the distinct molecular mechanisms of AMPK regulation by AMP and A769662. | ||
+ | |||
+ | Structural Basis for AMPK Activation: Natural and Synthetic Ligands Regulate Kinase Activity from Opposite Poles by Different Molecular Mechanisms.,Calabrese MF, Rajamohan F, Harris MS, Caspers NL, Magyar R, Withka JM, Wang H, Borzilleri KA, Sahasrabudhe PV, Hoth LR, Geoghegan KF, Han S, Brown J, Subashi TA, Reyes AR, Frisbie RK, Ward J, Miller RA, Landro JA, Londregan AT, Carpino PA, Cabral S, Smith AC, Conn EL, Cameron KO, Qiu X, Kurumbail RG Structure. 2014 Aug 5;22(8):1161-72. doi: 10.1016/j.str.2014.06.009. Epub 2014, Jul 24. PMID:25066137<ref>PMID:25066137</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 06:40, 13 August 2014
Structure of AMPK in complex with Cl-A769662 activator and STAUROSPORINE inhibitor
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