Crystal structure of human PNP complexed with hypoxanthine and sulfate ion.
Purine nucleoside phosphorylase (PNP) is a ubiquitous enzyme, which plays a key role in the purine salvage pathway, and PNP deficiency in humans leads to an impairment of T-cell function, usually with no apparent effects on B-cell function. Human PNP has been submitted to intensive structure-based design of inhibitors, most of them using low-resolution structures of human PNP. Here we report the crystal structure of human PNP in complex with hypoxanthine, refined to 2.6A resolution. The intermolecular interaction between ligand and PNP is discussed.
Canduri
Fernanda
F
Programa de Pós-graduação em Biofísica Molecular, Departamento de Física, UNESP, São José do Rio Preto, SP 15054-000, Brazil.
Fadel
Valmir
V
Dias
Marcio Vinícius Bertacine
MV
Basso
Luiz Augusto
LA
Palma
Mário Sérgio
MS
Santos
Diógenes Santiago
DS
de Azevedo
Walter Filgueira
WF
D018360:Crystallography, X-Ray; D006801:Humans; D019271:Hypoxanthine / Q000737:chemistry / Q000378:metabolism*; D007477:Ions / Q000737:chemistry / Q000378:metabolism; D008024:Ligands; D008958:Models, Molecular; D015394:Molecular Structure; D011487:Protein Conformation; D011683:Purine-Nucleoside Phosphorylase / Q000737:chemistry* / Q000378:metabolism*; D013431:Sulfates / Q000737:chemistry / Q000378:metabolism*
D007477:Ions; D008024:Ligands; D013431:Sulfates; D019271:Hypoxanthine; D011683:Purine-Nucleoside Phosphorylase