1Z0N
the glycogen-binding domain of the AMP-activated protein kinase
Summary for 1Z0N
| Entry DOI | 10.2210/pdb1z0n/pdb |
| Related | 1Z0M |
| Related PRD ID | PRD_900012 |
| Descriptor | 5'-AMP-activated protein kinase, beta-1 subunit, Cycloheptakis-(1-4)-(alpha-D-glucopyranose) (3 entities in total) |
| Functional Keywords | beta sandwich, sugar binding protein |
| Biological source | Rattus norvegicus (Norway rat) |
| Total number of polymer chains | 3 |
| Total formula weight | 36378.14 |
| Authors | Polekhina, G.,Gupta, A.,van Denderen, B.J.,Feil, S.C.,Kemp, B.E.,Stapleton, D.,Parker, M.W. (deposition date: 2005-03-02, release date: 2005-10-25, Last modification date: 2024-10-23) |
| Primary citation | Polekhina, G.,Gupta, A.,van Denderen, B.J.,Feil, S.C.,Kemp, B.E.,Stapleton, D.,Parker, M.W. Structural Basis for Glycogen Recognition by AMP-Activated Protein Kinase. Structure, 13:1453-1462, 2005 Cited by PubMed Abstract: 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. PubMed: 16216577DOI: 10.1016/j.str.2005.07.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.49 Å) |
Structure validation
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