4red
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Crystal structure of human AMPK alpha1 KD-AID with K43A mutation== |
| + | <StructureSection load='4red' size='340' side='right' caption='[[4red]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4red]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RED FirstGlance]. <br> | ||
| + | </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=4red FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4red OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4red RCSB], [http://www.ebi.ac.uk/pdbsum/4red PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | AMP-activated protein kinase (AMPK) is a central cellular energy sensor and regulator of energy homeostasis, and a promising drug target for the treatment of diabetes, obesity, and cancer. Here we present low-resolution crystal structures of the human alpha1beta2gamma1 holo-AMPK complex bound to its allosteric modulators AMP and the glycogen-mimic cyclodextrin, both in the phosphorylated (4.05 A) and non-phosphorylated (4.60 A) state. In addition, we have solved a 2.95 A structure of the human kinase domain (KD) bound to the adjacent autoinhibitory domain (AID) and have performed extensive biochemical and mutational studies. Together, these studies illustrate an underlying mechanism of allosteric AMPK modulation by AMP and glycogen, whose binding changes the equilibria between alternate AID (AMP) and carbohydrate-binding module (glycogen) interactions.Cell Research advance online publication 21 November 2014; doi:10.1038/cr.2014.150. | ||
| - | + | Structural basis of AMPK regulation by adenine nucleotides and glycogen.,Li X, Wang L, Zhou XE, Ke J, de Waal PW, Gu X, Tan MH, Wang D, Wu D, Xu HE, Melcher K Cell Res. 2014 Nov 21. doi: 10.1038/cr.2014.150. PMID:25412657<ref>PMID:25412657</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Gu, X]] | ||
| + | [[Category: Ke, J]] | ||
| + | [[Category: Li, X]] | ||
| + | [[Category: Melcher, K]] | ||
| + | [[Category: Tan, M H.E]] | ||
| + | [[Category: Waal, P De]] | ||
| + | [[Category: Wang, D]] | ||
| + | [[Category: Wang, L]] | ||
| + | [[Category: Wu, D]] | ||
| + | [[Category: Xu, H E]] | ||
| + | [[Category: Zhou, X E]] | ||
| + | [[Category: Ampk beta and gamma subunit]] | ||
| + | [[Category: Kinase domain fold]] | ||
| + | [[Category: Phosphorylate numerous cellular target]] | ||
| + | [[Category: Transferase]] | ||
| + | [[Category: Upregulate atp-generating pathways upon activation]] | ||
Revision as of 16:11, 10 December 2014
Crystal structure of human AMPK alpha1 KD-AID with K43A mutation
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