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New page: left|200px<br /> <applet load="1fc0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fc0, resolution 2.40Å" /> '''HUMAN LIVER GLYCOGE...
 
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[[Image:1fc0.gif|left|200px]]<br />
[[Image:1fc0.gif|left|200px]]<br /><applet load="1fc0" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1fc0" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1fc0, resolution 2.40&Aring;" />
caption="1fc0, resolution 2.40&Aring;" />
'''HUMAN LIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE'''<br />
'''HUMAN LIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE'''<br />


==Overview==
==Overview==
Glycogen phosphorylases catalyze the breakdown of glycogen to, glucose-1-phosphate, which enters glycolysis to fulfill the energetic, requirements of the organism. Maintaining control of blood glucose levels, is critical in minimizing the debilitating effects of diabetes, making, liver glycogen phosphorylase a potential therapeutic target. To support, inhibitor design, we determined the crystal structures of the active and, inactive forms of human liver glycogen phosphorylase a. During activation, forty residues of the catalytic site undergo order/disorder transitions, changes in secondary structure, or packing to reorganize the catalytic, site for substrate binding and catalysis. Knowing the inactive and active, conformations of the liver enzyme and how each differs from its, counterpart in muscle phosphorylase provides the basis for designing, inhibitors that bind preferentially to the inactive conformation of the, liver isozyme.
Glycogen phosphorylases catalyze the breakdown of glycogen to glucose-1-phosphate, which enters glycolysis to fulfill the energetic requirements of the organism. Maintaining control of blood glucose levels is critical in minimizing the debilitating effects of diabetes, making liver glycogen phosphorylase a potential therapeutic target. To support inhibitor design, we determined the crystal structures of the active and inactive forms of human liver glycogen phosphorylase a. During activation, forty residues of the catalytic site undergo order/disorder transitions, changes in secondary structure, or packing to reorganize the catalytic site for substrate binding and catalysis. Knowing the inactive and active conformations of the liver enzyme and how each differs from its counterpart in muscle phosphorylase provides the basis for designing inhibitors that bind preferentially to the inactive conformation of the liver isozyme.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1FC0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NBG 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FC0 OCA].  
1FC0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NBG:'>NBG</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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FC0 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ammirati, M.]]
[[Category: Ammirati, M.]]
[[Category: Danley, D.E.]]
[[Category: Danley, D E.]]
[[Category: Fennell, K.F.]]
[[Category: Fennell, K F.]]
[[Category: Hynes, T.R.]]
[[Category: Hynes, T R.]]
[[Category: LeMotte, P.K.]]
[[Category: LeMotte, P K.]]
[[Category: Mansour, M.M.]]
[[Category: Mansour, M M.]]
[[Category: Pandit, J.]]
[[Category: Pandit, J.]]
[[Category: Rath, V.L.]]
[[Category: Rath, V L.]]
[[Category: Schulte, G.K.]]
[[Category: Schulte, G K.]]
[[Category: Wasilko, D.J.]]
[[Category: Wasilko, D J.]]
[[Category: NBG]]
[[Category: NBG]]
[[Category: PLP]]
[[Category: PLP]]
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[[Category: phosphorylated protein]]
[[Category: phosphorylated protein]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:51:18 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:06 2008''