1nd5: Difference between revisions

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==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.

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==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: LaCount, M.W.]]

[[Category: LaCount, M W.]]

[[Category: Lebioda, L.]]

[[Category: Ortlund, E.]]

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[[Category: prostate]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: LaCount, M.W.]]
+[[Category: LaCount, M W.]]
 [[Category: Lebioda, L.]]
 [[Category: Ortlund, E.]]
@@ Line 27: / Line 27: @@
 [[Category: prostate]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:28:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:49 2008''