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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

The role of tryptophan 1072 in human PDE3B inhibitor binding.

The catalytic domain of recombinant human PDE3B was expressed in Escherichia coli as inclusion bodies and refolded to form active enzyme. A mutation at tryptophan 1072 in PDE3B disrupts inhibitor binding, but has minimal effect on cAMP hydrolysis. The W1072A mutation caused a 158-fold decrease in affinity for cilostamide, a 740-fold decrease for cGMP, and a 15-fold decrease in affinity for IBMX. The corresponding tyrosine mutation had a smaller effect. However, the K(m) of cAMP for the W1072A mutation was only increased by about 7-fold. The data indicate that the inhibitor binding region is not completely coincident with the substrate binding region. The homologous residue in PDE4B is located on helix 16 within 7A of the predicted bound substrate. A model of PDE3B was constructed based on the X-ray crystal structure of PDE4B.[1]

References

  1. The role of tryptophan 1072 in human PDE3B inhibitor binding. Chung, C., Varnerin, J.P., Morin, N.R., MacNeil, D.J., Singh, S.B., Patel, S., Scapin, G., Van der Ploeg, L.H., Tota, M.R. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
 
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