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1xc7

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[[Image:1xc7.gif|left|200px]]
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[[Image:1xc7.png|left|200px]]
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{{STRUCTURE_1xc7| PDB=1xc7 | SCENE= }}
{{STRUCTURE_1xc7| PDB=1xc7 | SCENE= }}
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'''Binding of beta-D-glucopyranosyl bismethoxyphosphoramidate to glycogen phosphorylase b: Kinetic and crystallographic studies'''
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===Binding of beta-D-glucopyranosyl bismethoxyphosphoramidate to glycogen phosphorylase b: Kinetic and crystallographic studies===
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==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.
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The line below this paragraph, {{ABSTRACT_PUBMED_15653344}}, adds the Publication Abstract to the page
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(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]
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:50:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:01:40 2008''

Revision as of 06:01, 28 July 2008

Image:1xc7.png

Template:STRUCTURE 1xc7

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

Template:ABSTRACT PUBMED 15653344

About this Structure

1XC7 is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

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: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:11895439

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