1xmu: Difference between revisions

Revision as of 08:17, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1xmu.png

Template:STRUCTURE 1xmu

Catalytic Domain Of Human Phosphodiesterase 4B In Complex With RoflumilastCatalytic Domain Of Human Phosphodiesterase 4B In Complex With Roflumilast

Template:ABSTRACT PUBMED 15576036

About this StructureAbout this Structure

1XMU is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the activity of drugs that inhibit phosphodiesterases., Card GL, England BP, Suzuki Y, Fong D, Powell B, Lee B, Luu C, Tabrizizad M, Gillette S, Ibrahim PN, Artis DR, Bollag G, Milburn MV, Kim SH, Schlessinger J, Zhang KY, Structure. 2004 Dec;12(12):2233-47. PMID:15576036

Page seeded by OCA on Mon Jul 28 08:17:41 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Catalytic Domain Of Human Phosphodiesterase 4B In Complex With Roflumilast'''
+===Catalytic Domain Of Human Phosphodiesterase 4B In Complex With Roflumilast===
-==Overview==
+<!--
-Phosphodiesterases (PDEs) comprise a large family of enzymes that catalyze the hydrolysis of cAMP or cGMP and are implicated in various diseases. We describe the high-resolution crystal structures of the catalytic domains of PDE4B, PDE4D, and PDE5A with ten different inhibitors, including the drug candidates cilomilast and roflumilast, for respiratory diseases. These cocrystal structures reveal a common scheme of inhibitor binding to the PDEs: (i) a hydrophobic clamp formed by highly conserved hydrophobic residues that sandwich the inhibitor in the active site; (ii) hydrogen bonding to an invariant glutamine that controls the orientation of inhibitor binding. A scaffold can be readily identified for any given inhibitor based on the formation of these two types of conserved interactions. These structural insights will enable the design of isoform-selective inhibitors with improved binding affinity and should facilitate the discovery of more potent and selective PDE inhibitors for the treatment of a variety of diseases.
+The line below this paragraph, {{ABSTRACT_PUBMED_15576036}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15576036}}
 ==About this Structure==
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 [[Category: Phosphodiesterase]]
 [[Category: Roflumilast]]
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