2fhy: Difference between revisions
New page: left|200px<br /> <applet load="2fhy" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fhy, resolution 2.95Å" /> '''Structure of human ... |
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[[Image:2fhy.gif|left|200px]]<br /> | [[Image:2fhy.gif|left|200px]]<br /><applet load="2fhy" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2fhy" size=" | |||
caption="2fhy, resolution 2.95Å" /> | caption="2fhy, resolution 2.95Å" /> | ||
'''Structure of human liver FPBase complexed with a novel benzoxazole as allosteric inhibitor'''<br /> | '''Structure of human liver FPBase complexed with a novel benzoxazole as allosteric inhibitor'''<br /> | ||
==Overview== | ==Overview== | ||
We have identified benzoxazole benzenesulfonamide 1 as a novel allosteric | We have identified benzoxazole benzenesulfonamide 1 as a novel allosteric inhibitor of fructose-1,6-bisphosphatase (FBPase-1). X-ray crystallographic and biological studies of 1 indicate a distinct binding mode that recapitulates features of several previously reported FBPase-1 inhibitor classes. | ||
==Disease== | ==Disease== | ||
Known disease associated with this structure: Fructose- | Known disease associated with this structure: Fructose-1,6-bidphosphatase deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=611570 611570]] | ||
==About this Structure== | ==About this Structure== | ||
2FHY 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 MG and A37 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] Full crystallographic information is available from [http:// | 2FHY 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=MG:'>MG</scene> and <scene name='pdbligand=A37:'>A37</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FHY OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: intersubunit allosteric inhibition of human fpbase]] | [[Category: intersubunit allosteric inhibition of human fpbase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:21:36 2008'' | ||
Revision as of 15:21, 21 February 2008
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Structure of human liver FPBase complexed with a novel benzoxazole as allosteric inhibitor
Overview
We have identified benzoxazole benzenesulfonamide 1 as a novel allosteric inhibitor of fructose-1,6-bisphosphatase (FBPase-1). X-ray crystallographic and biological studies of 1 indicate a distinct binding mode that recapitulates features of several previously reported FBPase-1 inhibitor classes.
Disease
Known disease associated with this structure: Fructose-1,6-bidphosphatase deficiency OMIM:[611570]
About this Structure
2FHY is a Single protein structure of sequence from Homo sapiens with MG and A37 as ligands. Active as Fructose-bisphosphatase, with EC number 3.1.3.11 Full crystallographic information is available from OCA.
Reference
Benzoxazole benzenesulfonamides are novel allosteric inhibitors of fructose-1,6-bisphosphatase with a distinct binding mode., von Geldern TW, Lai C, Gum RJ, Daly M, Sun C, Fry EH, Abad-Zapatero C, Bioorg Med Chem Lett. 2006 Apr 1;16(7):1811-5. Epub 2006 Jan 25. PMID:16442285
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