Prostatic acid phosphatase: structural aspects of inhibition by L-(+)-tartrate ions.
The crystal structure of the complex between rat-prostatic acid phosphatase (PAP) and L-(+)-tartrate (Lindqvist et al., J. Biol. Chem., 1993, 268, 20744-20746) contains the model of the ligand with incorrect chirality. We report here the correct model and discuss the relation between this model and the model of the inhibitory complexes between PAP and oxy-anions.
Lovelace
L
L
Department of Chemistry and Biochemistry, University of South Carolina, Columbia 29208, USA.
Lewiński
K
K
Jakob
C G
CG
Kuciel
R
R
Ostrowski
W
W
Lebioda
L
L
D000135:Acid Phosphatase / Q000037:antagonists & inhibitors* / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D006860:Hydrogen Bonding; D066298:In Vitro Techniques; D008024:Ligands; D008297:Male; D008958:Models, Molecular; D011467:Prostate / Q000201:enzymology*; D011487:Protein Conformation; D051381:Rats; D055672:Static Electricity; D013237:Stereoisomerism; D013644:Tartrates / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*
D004791:Enzyme Inhibitors; D008024:Ligands; D013644:Tartrates; D000135:Acid Phosphatase; C029768:tartaric acid