2hd1: Difference between revisions
New page: left|200px<br /><applet load="2hd1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hd1, resolution 2.23Å" /> '''Crystal structure of... |
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[[Image:2hd1.gif|left|200px]]<br /><applet load="2hd1" size=" | [[Image:2hd1.gif|left|200px]]<br /><applet load="2hd1" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2hd1, resolution 2.23Å" /> | caption="2hd1, resolution 2.23Å" /> | ||
'''Crystal structure of PDE9 in complex with IBMX'''<br /> | '''Crystal structure of PDE9 in complex with IBMX'''<br /> | ||
==Overview== | ==Overview== | ||
Cyclic nucleotide phosphodiesterases (PDEs) are enzymes controlling | Cyclic nucleotide phosphodiesterases (PDEs) are enzymes controlling cellular concentrations of the second messengers cAMP and cGMP. The crystal structure of the catalytic domain of PDE9A2, a member of a PDE family specifically hydrolyzing cGMP, has been determined at 2.23-A resolution. The PDE9A2 catalytic domain closely resembles the cAMP-specific PDE4D2 but is significantly different from the cGMP-specific PDE5A1, implying that each individual PDE family has its own characteristic substrate recognition mechanism. The different conformations of the H and M loops between PDE9A2 and PDE5A1 imply their less critical roles in nucleotide recognition. The nonselective inhibitor 3-isobutyl-1-methylxanthine (IBMX) binds to a similar subpocket in the active sites of PDE4, PDE5, and PDE9 and has a common pattern of the binding. However, significantly different orientations and interactions of IBMXs are observed among the three PDE families and also between two monomers of the PDE9A2 dimer. The kinetic properties of the PDE9A2 catalytic domain similar to those of full-length PDE9A imply that the N-terminal regulatory domain does not significantly alter the catalytic activity and the IBMX inhibition. | ||
==About this Structure== | ==About this Structure== | ||
2HD1 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, MG and IBM as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | 2HD1 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>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=IBM:'>IBM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1TBM. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HD1 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Colman, R | [[Category: Colman, R W.]] | ||
[[Category: Huai, Q.]] | [[Category: Huai, Q.]] | ||
[[Category: Ke, H.]] | [[Category: Ke, H.]] | ||
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[[Category: pde9]] | [[Category: pde9]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:40:37 2008'' | ||
Revision as of 18:40, 21 February 2008
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Crystal structure of PDE9 in complex with IBMX
OverviewOverview
Cyclic nucleotide phosphodiesterases (PDEs) are enzymes controlling cellular concentrations of the second messengers cAMP and cGMP. The crystal structure of the catalytic domain of PDE9A2, a member of a PDE family specifically hydrolyzing cGMP, has been determined at 2.23-A resolution. The PDE9A2 catalytic domain closely resembles the cAMP-specific PDE4D2 but is significantly different from the cGMP-specific PDE5A1, implying that each individual PDE family has its own characteristic substrate recognition mechanism. The different conformations of the H and M loops between PDE9A2 and PDE5A1 imply their less critical roles in nucleotide recognition. The nonselective inhibitor 3-isobutyl-1-methylxanthine (IBMX) binds to a similar subpocket in the active sites of PDE4, PDE5, and PDE9 and has a common pattern of the binding. However, significantly different orientations and interactions of IBMXs are observed among the three PDE families and also between two monomers of the PDE9A2 dimer. The kinetic properties of the PDE9A2 catalytic domain similar to those of full-length PDE9A imply that the N-terminal regulatory domain does not significantly alter the catalytic activity and the IBMX inhibition.
About this StructureAbout this Structure
2HD1 is a Single protein structure of sequence from Homo sapiens with , and as ligands. This structure supersedes the now removed PDB entry 1TBM. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of phosphodiesterase 9 shows orientation variation of inhibitor 3-isobutyl-1-methylxanthine binding., Huai Q, Wang H, Zhang W, Colman RW, Robinson H, Ke H, Proc Natl Acad Sci U S A. 2004 Jun 29;101(26):9624-9. Epub 2004 Jun 21. PMID:15210993
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