2hpa
From Proteopedia
|
STRUCTURAL ORIGINS OF L(+)-TARTRATE INHIBITION OF HUMAN PROSTATIC ACID PHOSPHATASE
Overview
Acid phosphatase activity in the blood serum is usually separated into, tartrate-resistant and tartrate-refractory, which is reported as the, prostatic acid phosphatase level. Human prostatic acid phosphatase, crystals soaked in N-propyl-L-tartramate were used to collect x-ray, diffraction data to 2.9 A resolution under cryogenic conditions. Positive, difference electron density, corresponding to the inhibitor, was found., The quality of the electron density maps clearly shows the orientation of, the carboxylate and N-propyl-substituted amide groups. The hydroxyl group, attached to C3 forms two crucial hydrogen bonds with Arg-79 and His-257., Previous crystallographic studies compiled on the tartrate-rat prostatic, acid phosphatase binary complex (Lindqvist, Y., Schneider, G., and Vihko, P. (1993) J. Biol. Chem. 268, 20744-20746) erroneously positioned, D-tartrate into the active site. Modeling studies have shown that the C3, hydroxyl group on the D(-)-stereoisomer of tartrate, which does not, significantly inhibit prostatic acid phosphatase, does not form strong, hydrogen bonds with Arg-79 or His-257. The structure of human prostatic, acid phosphatase, noncovalently bound in N-propyl-L-tartramate, is used to, develop inhibitors with higher specificity and potency than L(+)-tartrate.
About this Structure
2HPA is a Single protein structure of sequence from Homo sapiens with NAG, NDG and PT3 as ligands. Active as Acid phosphatase, with EC number 3.1.3.2 Full crystallographic information is available from OCA.
Reference
Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase., LaCount MW, Handy G, Lebioda L, J Biol Chem. 1998 Nov 13;273(46):30406-9. PMID:9804805
Page seeded by OCA on Mon Nov 12 22:34:51 2007
Categories: Acid phosphatase | Homo sapiens | Single protein | Handy, G. | Lacount, M.W. | Lebioda, L. | NAG | NDG | PT3 | N-propyltartramate
