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2prj

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{{STRUCTURE_2prj| PDB=2prj | SCENE= }}
{{STRUCTURE_2prj| PDB=2prj | SCENE= }}
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'''Binding of N-acetyl-beta-D-glucopyranosylamine to Glycogen Phosphorylase B'''
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===Binding of N-acetyl-beta-D-glucopyranosylamine to Glycogen Phosphorylase B===
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==Overview==
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Structure-based drug design has led to the discovery of a number of glucose analogue inhibitors of glycogen phosphorylase that have an increased affinity compared to alpha-D-glucose (Ki = 1.7 mM). The best inhibitor in the class of N-acyl derivatives of beta-D-glucopyranosylamine, N-acetyl-beta-D-glucopyranosylamine (1-GlcNAc), has been characterized by kinetic, ultracentrifugation, and crystallographic studies. 1-GlcNAc acts as a competitive inhibitor for both the b (Ki = 32 microM) and the a (Ki = 35 microM) forms of the enzyme with respect to glucose 1-phosphate and in synergism with caffeine, mimicking the binding of glucose. Sedimentation velocity experiments demonstrated that 1-GlcNAc was able to induce dissociation of tetrameric phosphorylase a and stabilization of the dimeric T-state conformation. Co-crystals of the phosphorylase b-1-GlcNAc-IMP complex were grown in space group P4(3)2(1)2, with native-like unit cell dimensions, and the complex structure has been refined to give a crystallographic R factor of 18.1%, for data between 8 and 2.3 A resolution. 1-GlcNAc binds tightly at the catalytic site of T-state phosphorylase b at approximately the same position as that of alpha-D-glucose. The ligand can be accommodated in the catalytic site with very little change in the protein structure and stabilizes the T-state conformation of the 280s loop by making several favorable contacts to Asn 284 of this loop. Structural comparisons show that the T-state phosphorylase b-1-GlcNAc-IMP complex structure is overall similar to the T-state phosphorylase b-alpha-D-glucose complex structure. The structure of the 1-GlcNAc complex provides a rational for the biochemical properties of the inhibitor.
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{{ABSTRACT_PUBMED_8580837}}
==About this Structure==
==About this Structure==
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[[Category: Zographos, S E.]]
[[Category: Zographos, S E.]]
[[Category: Glycogen phosphorylase]]
[[Category: Glycogen phosphorylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:39:24 2008''

Revision as of 05:39, 28 July 2008

Image:2prj.png

Template:STRUCTURE 2prj

Binding of N-acetyl-beta-D-glucopyranosylamine to Glycogen Phosphorylase B

Template:ABSTRACT PUBMED 8580837

About this Structure

2PRJ is a Single protein structure of sequence from Oryctolagus cuniculus. This structure supersedes the now removed PDB entry 1prj. Full crystallographic information is available from OCA.

Reference

N-acetyl-beta-D-glucopyranosylamine: a potent T-state inhibitor of glycogen phosphorylase. A comparison with alpha-D-glucose., Oikonomakos NG, Kontou M, Zographos SE, Watson KA, Johnson LN, Bichard CJ, Fleet GW, Acharya KR, Protein Sci. 1995 Dec;4(12):2469-77. PMID:8580837

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