1xc7: Difference between revisions

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[[Image:1xc7.gif|left|200px]]
{{Seed}}
[[Image:1xc7.png|left|200px]]


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{{STRUCTURE_1xc7|  PDB=1xc7  |  SCENE=  }}  
{{STRUCTURE_1xc7|  PDB=1xc7  |  SCENE=  }}  


'''Binding of beta-D-glucopyranosyl bismethoxyphosphoramidate to glycogen phosphorylase b: Kinetic and crystallographic studies'''
===Binding of beta-D-glucopyranosyl bismethoxyphosphoramidate to glycogen phosphorylase b: Kinetic and crystallographic studies===




==Overview==
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In an attempt to identify a new lead molecule that would enable the design of inhibitors with enhanced affinity for glycogen phosphorylase (GP), beta-D-glucopyranosyl bismethoxyphosphoramidate (phosphoramidate), a glucosyl phosphate analogue, was tested for inhibition of the enzyme. Kinetic experiments showed that the compound was a weak competitive inhibitor of rabbit muscle GPb (with respect to alpha-D-glucose-1-phosphate (Glc-1-P)) with a Ki value of 5.9 (+/-0.1) mM. In order to elucidate the structural basis of inhibition, we determined the structure of GPb complexed with the phosphoramidate at 1.83 A resolution. The complex structure reveals that the inhibitor binds at the catalytic site and induces significant conformational changes in the vicinity of this site. In particular, the 280s loop (residues 282-287) shifts 0.4-4.3 A (main-chain atoms) to accommodate the phosphoramidate, but these conformational changes do not lead to increased contacts between the inhibitor and the protein that would improve ligand binding.
The line below this paragraph, {{ABSTRACT_PUBMED_15653344}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15653344 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15653344}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Binding of beta-D-glucopyranosyl bismethoxyphosphoramidate to glycogen phosphorylase b: kinetic and crystallographic studies., Chrysina ED, Kosmopoulou MN, Kardakaris R, Bischler N, Leonidas DD, Kannan T, Loganathan D, Oikonomakos NG, Bioorg Med Chem. 2005 Feb 1;13(3):765-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15653344 15653344]
Binding of beta-D-glucopyranosyl bismethoxyphosphoramidate to glycogen phosphorylase b: kinetic and crystallographic studies., Chrysina ED, Kosmopoulou MN, Kardakaris R, Bischler N, Leonidas DD, Kannan T, Loganathan D, Oikonomakos NG, Bioorg Med Chem. 2005 Feb 1;13(3):765-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15653344 15653344]
Binding of N-acetyl-N '-beta-D-glucopyranosyl urea and N-benzoyl-N '-beta-D-glucopyranosyl urea to glycogen phosphorylase b: kinetic and crystallographic studies., Oikonomakos NG, Kosmopoulou M, Zographos SE, Leonidas DD, Chrysina ED, Somsak L, Nagy V, Praly JP, Docsa T, Toth B, Gergely P, Eur J Biochem. 2002 Mar;269(6):1684-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11895439 11895439]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Phosphorylase]]
[[Category: Phosphorylase]]
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[[Category: Glycogenolysis]]
[[Category: Glycogenolysis]]
[[Category: Type 2 diabetes]]
[[Category: Type 2 diabetes]]
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