4rew: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of the non-phosphorylated human alpha1 beta2 gamma1 holo-AMPK complex==
<StructureSection load='4rew' size='340' side='right' caption='[[4rew]], [[Resolution|resolution]] 4.58&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4rew]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4REW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4REW FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=STU:STAUROSPORINE'>STU</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4red|4red]], [[4rer|4rer]]</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=4rew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rew OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rew RCSB], [http://www.ebi.ac.uk/pdbsum/4rew 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.


The entry 4rew is ON HOLD
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>


Authors: Zhou, X.E., Ke, J., Li, X., Wang, L., Gu, X., De Waal, P., Tan, M.H.E., Wang, D., Wu, D., Xu, H.E., Melcher, K.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Crystal structure of the non-phosphorylated human alpha1 beta2 gamma1 holo-AMPK complex
== 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: Axin]]
[[Category: Camkkbeta]]
[[Category: Glycogen]]
[[Category: Human alpha1 beta2 gamma1 holo-ampk complex]]
[[Category: Lkb1]]
[[Category: Phosphorylation]]
[[Category: Serine/threonine protein kinase]]
[[Category: Transferase]]

Revision as of 19:00, 10 December 2014

Crystal structure of the non-phosphorylated human alpha1 beta2 gamma1 holo-AMPK complexCrystal structure of the non-phosphorylated human alpha1 beta2 gamma1 holo-AMPK complex

Structural highlights

4rew is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, RCSB, PDBsum

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[1]

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

References

  1. ↑ Li X, Wang L, Zhou XE, Ke J, de Waal PW, Gu X, Tan MH, Wang D, Wu D, Xu HE, Melcher K. Structural basis of AMPK regulation by adenine nucleotides and glycogen. Cell Res. 2014 Nov 21. doi: 10.1038/cr.2014.150. PMID:25412657 doi:http://dx.doi.org/10.1038/cr.2014.150

4rew, resolution 4.58Å

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