1ptw

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[[Image:1ptw.jpg|left|200px]]
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{{Seed}}
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{{STRUCTURE_1ptw| PDB=1ptw | SCENE= }}
{{STRUCTURE_1ptw| PDB=1ptw | SCENE= }}
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'''The Crystal Structure of AMP-Bound PDE4 Suggests a Mechanism for Phosphodiesterase Catalysis'''
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===The Crystal Structure of AMP-Bound PDE4 Suggests a Mechanism for Phosphodiesterase Catalysis===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 14609333 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14609333}}
==About this Structure==
==About this Structure==
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[[Category: Camp hydrolysis crystal structure]]
[[Category: Camp hydrolysis crystal structure]]
[[Category: Catalytic mechanism]]
[[Category: Catalytic mechanism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:28:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:22:12 2008''

Revision as of 09:22, 28 July 2008

Image:1ptw.png

Template:STRUCTURE 1ptw

The Crystal Structure of AMP-Bound PDE4 Suggests a Mechanism for Phosphodiesterase Catalysis

Template:ABSTRACT PUBMED 14609333

About this Structure

1PTW is a Single protein structure of sequence from Homo sapiens. 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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