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Literature summary for 2.4.2.1 extracted from

  • Edwards, A.A.; Tipton, J.D.; Brenowitz, M.D.; Emmett, M.R.; Marshall, A.G.; Evans, G.B.; Tyler, P.C.; Schramm, V.L.
    Conformational States of human purine nucleoside phosphorylase at rest, at work, and with transition state analogues (2010), Biochemistry, 49, 2058-2067.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
conformational states in complex with transition state analogues Immucillin-H and DATMe-Immucillin-H. The (purine nucelotide phosphorylase)3(PO4)3 ImmH-complex is more compact by sedimentation rate than the other complexes. Purine nucelotide phosphorylase protein conformation of dynamic motion correlates more closely with entropy of binding than with affinity. Catalytically active turnover with saturated substrate sites causes less change in peptide amide deuterium exchange and sedimentation rates than binding of transition state analogues. DATMe-Immucilin-H more closely mimics the transition of human PNP than does Immucilin-H and achieves strong binding interactions at the catalytic site while causing relatively modest alterations of the protein dynamic motion Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P00491
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