1nd6

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spinqualitylabelsall models 1nd6, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion and alpha-Benzylaminobenzylphosphonic Acid Update the Mechanistic Picture and Offer New Insights into Inhibitor Design

Overview

The X-ray crystal structure of human prostatic acid phosphatase (PAP) in, complex with a phosphate ion has been determined at 2.4 A resolution. This, structure offers a snapshot of the final intermediate in the catalytic, mechanism and does not support the role of Asp 258 as a proton donor in, catalysis. A total of eight hydrogen bonds serve to strongly bind the, phosphate ion within the active site. Bound PEG molecules from the, crystallization matrix have allowed the identification of a channel within, the molecule that likely plays a role in molecular recognition and in, macromolecular substrate selectivity. Additionally, the structure of PAP, in complex with a phosphate derivative, alpha-benzylaminobenzylphosphonic, acid, a potent inhibitor (IC(50) = 4 nM), has been determined to 2.9 A, resolution. This structure gives new insight into the determinants of, binding hydrophobic ligands within the active site and allows us to, explain PAP's preference for aromatic substrates.

About this Structure

1ND6 is a Single protein structure of sequence from Homo sapiens with NAG, PO4, GLY and 1PE as ligands. Active as Acid phosphatase, with EC number 3.1.3.2 Full crystallographic information is available from OCA.

Reference

Crystal structures of human prostatic acid phosphatase in complex with a phosphate ion and alpha-benzylaminobenzylphosphonic acid update the mechanistic picture and offer new insights into inhibitor design., Ortlund E, LaCount MW, Lebioda L, Biochemistry. 2003 Jan 21;42(2):383-9. PMID:12525165

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