Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of R-state glycogen phosphorylase b has been determined at 2.9 A resolution. A comparison of T-state and R-state structures of the enzyme explains its cooperative behaviour on ligand binding and the allosteric regulation of its activity. Communication between catalytic sites of the dimer is provided by a change in packing geometry of two helices linking each site with the subunit interface. Activation by AMP or by phosphorylation results in a quaternary conformational change that switches these two helices into the R-state conformation.
The allosteric transition of glycogen phosphorylase.,Barford D, Johnson LN Nature. 1989 Aug 24;340(6235):609-16. PMID:2770867[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Barford D, Johnson LN. The allosteric transition of glycogen phosphorylase. Nature. 1989 Aug 24;340(6235):609-16. PMID:2770867 doi:http://dx.doi.org/10.1038/340609a0
