2fhy

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(New page: 200px<br /> <applet load="2fhy" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fhy, resolution 2.95&Aring;" /> '''Structure of human ...)
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[[Image:2fhy.gif|left|200px]]<br />
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[[Image:2fhy.gif|left|200px]]<br /><applet load="2fhy" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2fhy" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2fhy, resolution 2.95&Aring;" />
caption="2fhy, resolution 2.95&Aring;" />
'''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==
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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.
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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==
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Known disease associated with this structure: Fructose-bisphosphatase deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=229700 229700]]
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FHY OCA].
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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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:05:36 2007''
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''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


2fhy, resolution 2.95Å

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Structure of human liver FPBase complexed with a novel benzoxazole as allosteric inhibitor

Contents

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 and 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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