2Q7O

Structure of human purine nucleoside phosphorylase in complex with L-Immucillin-H

Summary for 2Q7O

• Entry DOI: 10.2210/pdb2q7o/pdb
• Related: 1rr6
• Descriptor: Purine nucleoside phosphorylase, PHOSPHATE ION, 1,4-DIDEOXY-4-AZA-1-(S)-(9-DEAZAHYPOXANTHIN-9-YL)-D-RIBITOL, ... (4 entities in total)
• Functional Keywords: purine nucleoside phosphorylase, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton : P00491
• Total number of polymer chains: 1
• Total formula weight: 32546.10

Authors

Rinaldo-Matthis, A.,Almo, S.C.,Schramm, V.L. (deposition date: 2007-06-07, release date: 2008-01-15, Last modification date: 2023-08-30)

Primary citation

Rinaldo-Matthis, A.,Murkin, A.S.,Ramagopal, U.A.,Clinch, K.,Mee, S.P.,Evans, G.B.,Tyler, P.C.,Furneaux, R.H.,Almo, S.C.,Schramm, V.L.
L-Enantiomers of transition state analogue inhibitors bound to human purine nucleoside phosphorylase.
J.Am.Chem.Soc., 130:842-844, 2008

PubMed Abstract: Human purine nucleoside phosphorylase (PNP) was crystallized with transition-state analogue inhibitors Immucillin-H and DADMe-Immucillin-H synthesized with ribosyl mimics of l-stereochemistry. The inhibitors demonstrate that major driving forces for tight binding of these analogues are the leaving group interaction and the cationic mimicry of the transition state, even though large geometric changes occur with d-Immucillins and l-Immucillins bound to human PNP.

PubMed: 18154341
DOI: 10.1021/ja710733g

Experimental method

X-RAY DIFFRACTION (2.9 Å)