Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2005-6-30
pubmed:abstractText
Selective inhibitors of cyclic nucleotide phosphodiesterases (PDEs) have been widely studied as therapeutic agents for the treatment of various human diseases. Three-dimensional structures are essential for the design of highly selective inhibitors, but their availability is limited by the speed of crystallization. We describe crystallization of the catalytic domains of the unligated PDE4B2B, rolipram-bound PDE4D2, and 3-isobutyl-1-methylxanthine-bound PDE5A1 using the methods of vapor diffusion and microdialysis. We also briefly describe general methods of protein crystallization to provide a background to readers outside of the crystallographic field. Finally, we discuss detailed procedures for and pitfalls of the crystallization of PDEs, which may be valuable for crystallization of other PDE members.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1064-3745
pubmed:author
pubmed:issnType
Print
pubmed:volume
307
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
181-90
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Crystallization of cyclic nucleotide phosphodiesterases.
pubmed:affiliation
Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, USA.
pubmed:publicationType
Journal Article