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Literature summary for 2.4.2.1 extracted from

  • Ho, M.C.; Shi, W.; Rinaldo-Matthis, A.; Tyler, P.C.; Evans, G.B.; Clinch, K.; Almo, S.C.; Schramm, V.L.
    Four generations of transition-state analogues for human purine nucleoside phosphorylase (2010), Proc. Natl. Acad. Sci. USA, 107, 4805-4812.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with transition-state analogues immucillin-H, DADMe-immucillin-H, DATMe-immucillin-H, and immucillin-H, to 2.4 A to 2.5 A resolution. Inhibitor binding sites of purine nucelotide phosphorylase are near the C-terminal region of the 6-stranded beta-sheet. The purine base binding region consists primarily of hydrophobic residues including Phe200, Val217, Met219, Val245, and Val260. Purine base interactions also include the polar residues Glu201 and Asn243 as hydrogen bond acceptors from the NH1 and NH7 groups of 9-deazahypoxanthine. Asn243 also donates hydrogen bonds to O6 of the deazapurine, except in the case of immucillin-H. Features of tight binding are ion-pair formation between bound phosphate or its mimic and inhibitor cation, leaving-group interactions to N1, O6, and N7 of 9-deazahypoxanthine, interaction between phosphate and inhibitor hydroxyl groups, and His257 interacting with the 5'-hydroxyl group Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
DADMe-immucillin-H
-
Homo sapiens
DATMe-immucillin-H
-
Homo sapiens
immucillin-H
-
Homo sapiens
SerMe-immucillin-H
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P00491
-
-