1z0m
From Proteopedia
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| - | [[Image:1z0m.gif|left|200px]] | + | [[Image:1z0m.gif|left|200px]] |
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| - | '''the glycogen-binding domain of the AMP-activated protein kinase beta1 subunit''' | + | {{Structure |
| + | |PDB= 1z0m |SIZE=350|CAPTION= <scene name='initialview01'>1z0m</scene>, resolution 1.910Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=BCD:BETA-CYCLODEXTRIN'>BCD</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''the glycogen-binding domain of the AMP-activated protein kinase beta1 subunit''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Z0M is a [ | + | 1Z0M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0M OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for glycogen recognition by AMP-activated protein kinase., Polekhina G, Gupta A, van Denderen BJ, Feil SC, Kemp BE, Stapleton D, Parker MW, Structure. 2005 Oct;13(10):1453-62. PMID:[http:// | + | Structural basis for glycogen recognition by AMP-activated protein kinase., Polekhina G, Gupta A, van Denderen BJ, Feil SC, Kemp BE, Stapleton D, Parker MW, Structure. 2005 Oct;13(10):1453-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16216577 16216577] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: beta sandwich]] | [[Category: beta sandwich]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:29:49 2008'' |
Revision as of 13:29, 20 March 2008
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| , resolution 1.910Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
the glycogen-binding domain of the AMP-activated protein kinase beta1 subunit
Overview
AMP-activated protein kinase (AMPK) coordinates cellular metabolism in response to energy demand as well as to a variety of stimuli. The AMPK beta subunit acts as a scaffold for the alpha catalytic and gamma regulatory subunits and targets the AMPK heterotrimer to glycogen. We have determined the structure of the AMPK beta glycogen binding domain in complex with beta-cyclodextrin. The structure reveals a carbohydrate binding pocket that consolidates all known aspects of carbohydrate binding observed in starch binding domains into one site, with extensive contact between several residues and five glucose units. beta-cyclodextrin is held in a pincer-like grasp with two tryptophan residues cradling two beta-cyclodextrin glucose units and a leucine residue piercing the beta-cyclodextrin ring. Mutation of key beta-cyclodextrin binding residues either partially or completely prevents the glycogen binding domain from binding glycogen. Modeling suggests that this binding pocket enables AMPK to interact with glycogen anywhere across the carbohydrate's helical surface.
About this Structure
1Z0M is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structural basis for glycogen recognition by AMP-activated protein kinase., Polekhina G, Gupta A, van Denderen BJ, Feil SC, Kemp BE, Stapleton D, Parker MW, Structure. 2005 Oct;13(10):1453-62. PMID:16216577
Page seeded by OCA on Thu Mar 20 15:29:49 2008
