1ula
From Proteopedia
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APPLICATION OF CRYSTALLOGRAPHIC AND MODELING METHODS IN THE DESIGN OF PURINE NUCLEOSIDE PHOSPHORYLASE INHIBITORS
Contents |
Overview
Competitive inhibitors of the salvage pathway enzyme purine-nucleoside, phosphorylase (purine-nucleoside:orthophosphate ribosyltransferase, EC, 2.4.2.1) have been designed by using the three-dimensional structure of, the enzyme as determined by x-ray crystallography. The process was an, iterative one that utilized interactive computer graphics, Monte, Carlo-based conformational searching, energy minimization, and x-ray, crystallography. The proposed compounds were synthesized and tested by an, in vitro assay. Among the compounds designed and synthesized are the most, potent competitive inhibitors of purine nucleoside phosphorylase thus far, reported.
Disease
Known diseases associated with this structure: Neutral lipid storage disease with myopathy OMIM:[609059], Nucleoside phosphorylase deficiency, immunodeficiency due to OMIM:[164050]
About this Structure
1ULA is a Single protein structure of sequence from Homo sapiens with as ligand. This structure superseeds the now removed PDB entry 2PNP. Active as Purine-nucleoside phosphorylase, with EC number 2.4.2.1 Full crystallographic information is available from OCA.
Reference
Application of crystallographic and modeling methods in the design of purine nucleoside phosphorylase inhibitors., Ealick SE, Babu YS, Bugg CE, Erion MD, Guida WC, Montgomery JA, Secrist JA 3rd, Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11540-4. PMID:1763067
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