This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1h5u
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1h5u.gif|left|200px]]<br /><applet load="1h5u" size=" | + | [[Image:1h5u.gif|left|200px]]<br /><applet load="1h5u" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1h5u, resolution 1.76Å" /> | caption="1h5u, resolution 1.76Å" /> | ||
'''THE 1.76 A RESOLUTION CRYSTAL STRUCTURE OF GLYCOGEN PHOSPHORYLASE B COMPLEXED WITH GLUCOSE AND CP320626, A POTENTIAL ANTIDIABETIC DRUG'''<br /> | '''THE 1.76 A RESOLUTION CRYSTAL STRUCTURE OF GLYCOGEN PHOSPHORYLASE B COMPLEXED WITH GLUCOSE AND CP320626, A POTENTIAL ANTIDIABETIC DRUG'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1H5U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with GLC, CHI and PLP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] Known structural/functional Sites: <scene name='pdbsite=CHI:Chi/Cp320626 Binding Site'>CHI</scene>, <scene name='pdbsite=GLC:Glc Binding Site For Chain A'>GLC</scene> and <scene name='pdbsite=PLP:Plp Binding Site For Chain A'>PLP</scene>. Full crystallographic information is available from [http:// | + | 1H5U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=GLC:'>GLC</scene>, <scene name='pdbligand=CHI:'>CHI</scene> and <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] Known structural/functional Sites: <scene name='pdbsite=CHI:Chi/Cp320626+Binding+Site'>CHI</scene>, <scene name='pdbsite=GLC:Glc+Binding+Site+For+Chain+A'>GLC</scene> and <scene name='pdbsite=PLP:Plp+Binding+Site+For+Chain+A'>PLP</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5U OCA]. |
==Reference== | ==Reference== | ||
| Line 28: | Line 28: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:46:49 2008'' |
Revision as of 07:46, 3 February 2008
|
THE 1.76 A RESOLUTION CRYSTAL STRUCTURE OF GLYCOGEN PHOSPHORYLASE B COMPLEXED WITH GLUCOSE AND CP320626, A POTENTIAL ANTIDIABETIC DRUG
Overview
CP320626, a potential antidiabetic drug, inhibits glycogen phosphorylase, in synergism with glucose. To elucidate the structural basis of, synergistic inhibition, we determined the structure of muscle glycogen, phosphorylase b (MGPb) complexed with both glucose and CP320626 at 1.76 A, resolution, and refined to a crystallographic R value of 0.211, (R(free)=0.235). CP320626 binds at a novel allosteric site, which is some, 33 A from the catalytic site, where glucose binds. The high resolution, structure allows unambiguous definition of the conformation of the, 1-acetyl-4-hydroxy-piperidine ring supported by theoretical energy, calculations. Both CP320626 and glucose promote the less active T-state, thereby explaining their synergistic inhibition. Structural comparison of, MGPb--glucose--CP320626 complex with liver glycogen phosphorylase a (LGPa), complexed with a related compound (CP403700) show that the ligand binding, site is conserved in LGPa.
About this Structure
1H5U is a Single protein structure of sequence from Oryctolagus cuniculus with , and as ligands. Active as Phosphorylase, with EC number 2.4.1.1 Known structural/functional Sites: , and . Full crystallographic information is available from OCA.
Reference
The 1.76 A resolution crystal structure of glycogen phosphorylase B complexed with glucose, and CP320626, a potential antidiabetic drug., Oikonomakos NG, Zographos SE, Skamnaki VT, Archontis G, Bioorg Med Chem. 2002 May;10(5):1313-9. PMID:11886794
Page seeded by OCA on Sun Feb 3 09:46:49 2008
