1ptw
From Proteopedia
(New page: 200px<br /> <applet load="1ptw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ptw, resolution 2.3Å" /> '''The Crystal Structur...) |
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caption="1ptw, resolution 2.3Å" /> | caption="1ptw, resolution 2.3Å" /> | ||
'''The Crystal Structure of AMP-Bound PDE4 Suggests a Mechanism for Phosphodiesterase Catalysis'''<br /> | '''The Crystal Structure of AMP-Bound PDE4 Suggests a Mechanism for Phosphodiesterase Catalysis'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PTW 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 ZN and AMP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] Full crystallographic information is available from [http:// | + | 1PTW 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=ZN:'>ZN</scene> and <scene name='pdbligand=AMP:'>AMP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PTW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: catalytic mechanism]] | [[Category: catalytic mechanism]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:41:36 2008'' |
Revision as of 14:41, 15 February 2008
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The Crystal Structure of AMP-Bound PDE4 Suggests a Mechanism for Phosphodiesterase Catalysis
Contents |
Overview
Cyclic nucleotide phosphodiesterases (PDEs) regulate the intracellular, concentrations of cyclic 3',5'-adenosine and guanosine monophosphates, (cAMP and cGMP, respectively) by hydrolyzing them to AMP and GMP, respectively. Family-selective inhibitors of PDEs have been studied for, treatment of various human diseases. However, the catalytic mechanism of, cyclic nucleotide hydrolysis by PDEs has remained unclear. We determined, the crystal structure of the human PDE4D2 catalytic domain in complex with, AMP at 2.4 A resolution. In this structure, two divalent metal ions, simultaneously interact with the phosphate group of AMP, implying a, binuclear catalysis. In addition, the structure suggested that a hydroxide, ion or a water bridging two metal ions may serve as the nucleophile for, the hydrolysis of the cAMP phosphodiester bond.
Disease
Known disease associated with this structure: Stroke, susceptibility to, 1 OMIM:[600129]
About this Structure
1PTW is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as 3',5'-cyclic-nucleotide phosphodiesterase, with EC number 3.1.4.17 Full crystallographic information is available from OCA.
Reference
The crystal structure of AMP-bound PDE4 suggests a mechanism for phosphodiesterase catalysis., Huai Q, Colicelli J, Ke H, Biochemistry. 2003 Nov 18;42(45):13220-6. PMID:14609333
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