1nd6
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The X-ray crystal structure of human prostatic acid phosphatase (PAP) in | + | 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== | ==About this Structure== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: LaCount, M | + | [[Category: LaCount, M W.]] |
[[Category: Lebioda, L.]] | [[Category: Lebioda, L.]] | ||
[[Category: Ortlund, E.]] | [[Category: Ortlund, E.]] | ||
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[[Category: prostatic acid phosphatase]] | [[Category: prostatic acid phosphatase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:50 2008'' |
Revision as of 12:04, 21 February 2008
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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 , , and 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
Page seeded by OCA on Thu Feb 21 14:04:50 2008
Categories: Acid phosphatase | Homo sapiens | Single protein | LaCount, M W. | Lebioda, L. | Ortlund, E. | 1PE | GLY | NAG | PO4 | Inhibitor | Pap | Phosphate | Prostate | Prostatic acid phosphatase
