1kz8

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[[Image:1kz8.gif|left|200px]]
[[Image:1kz8.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1kz8 |SIZE=350|CAPTION= <scene name='initialview01'>1kz8</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1kz8", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PFE:{4-[3-(6,7-DIETHOXY-QUINAZOLIN-4-YLAMINO)-PHENYL]-THIAZOL-2-YL}-METHANOL'>PFE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1kz8| PDB=1kz8 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kz8 OCA], [http://www.ebi.ac.uk/pdbsum/1kz8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kz8 RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF PORCINE FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH A NOVEL ALLOSTERIC-SITE INHIBITOR'''
'''CRYSTAL STRUCTURE OF PORCINE FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH A NOVEL ALLOSTERIC-SITE INHIBITOR'''
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[[Category: Wang, I K.]]
[[Category: Wang, I K.]]
[[Category: Wright, S W.]]
[[Category: Wright, S W.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:21:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:55:42 2008''
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Revision as of 20:21, 2 May 2008

Image:1kz8.gif

Template:STRUCTURE 1kz8

CRYSTAL STRUCTURE OF PORCINE FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH A NOVEL ALLOSTERIC-SITE INHIBITOR


Overview

The synthesis and in vitro structure-activity relationships (SAR) of a novel series of anilinoquinazolines as allosteric inhibitors of fructose-1,6-bisphosphatase (F16Bpase) are reported. The compounds have a different SAR as inhibitors of F16Bpase than anilinoquinazolines previously reported. Selective inhibition of F16Bpase can be attained through the addition of appropriate polar functional groups at the quinazoline 2-position, thus separating the F16Bpase inhibitory activity from the epidermal growth factor receptor tyrosine kinase inhibitory activity previously observed with similar structures. The compounds have been found to bind at a symmetry-repeated novel allosteric site at the subunit interface of the enzyme. Inhibition is brought about by binding to a loop comprised of residues 52-72, preventing the necessary participation of these residues in the assembly of the catalytic site. Mutagenesis studies have identified the key amino acid residues in the loop that are required for inhibitor recognition and binding.

About this Structure

1KZ8 is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Anilinoquinazoline inhibitors of fructose 1,6-bisphosphatase bind at a novel allosteric site: synthesis, in vitro characterization, and X-ray crystallography., Wright SW, Carlo AA, Carty MD, Danley DE, Hageman DL, Karam GA, Levy CB, Mansour MN, Mathiowetz AM, McClure LD, Nestor NB, McPherson RK, Pandit J, Pustilnik LR, Schulte GK, Soeller WC, Treadway JL, Wang IK, Bauer PH, J Med Chem. 2002 Aug 29;45(18):3865-77. PMID:12190310 Page seeded by OCA on Fri May 2 23:21:11 2008

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OCA

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