Journal:Acta Cryst F:S2053230X21008542
From Proteopedia
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
The crystal structures of the free T- and R-state glycogen phosphorylase (GP) and the R-state GP in complex with allosteric activators IMP and AMP are reported, in improved resolution. GP is a validated pharmaceutical target for the development of antihyperglycaemic agents and the reported structures can have significant impact on structure-based drug design efforts. Comparisons to previously reported structures of lower resolution reveal the detailed conformation of important structural features of the allosteric transition from T- to R-state of GP. | The crystal structures of the free T- and R-state glycogen phosphorylase (GP) and the R-state GP in complex with allosteric activators IMP and AMP are reported, in improved resolution. GP is a validated pharmaceutical target for the development of antihyperglycaemic agents and the reported structures can have significant impact on structure-based drug design efforts. Comparisons to previously reported structures of lower resolution reveal the detailed conformation of important structural features of the allosteric transition from T- to R-state of GP. | ||
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| + | The R-state rmGPb-AMP from a crystal grown in the presence of AMP: | ||
| + | *<scene name='89/890862/Cv/4'>Each tetramer is colored in different colour</scene> | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 13:57, 25 August 2021
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This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
