1h5u
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(New page: 200px<br /> <applet load="1h5u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h5u, resolution 1.76Å" /> '''THE 1.76 A RESOLUTI...)
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Revision as of 16:02, 29 October 2007
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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, ... [(full description)]
About this Structure
1H5U is a [Single protein] structure of sequence from [Oryctolagus cuniculus] with GLC, CHI and PLP as [ligands]. Active as [[1]], with EC number [2.4.1.1]. 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
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