1zed

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[[Image:1zed.gif|left|200px]]<br /><applet load="1zed" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1zed.gif|left|200px]]
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caption="1zed, resolution 1.57&Aring;" />
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'''Alkaline phosphatase from human placenta in complex with p-nitrophenyl-phosphonate'''<br />
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{{Structure
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|PDB= 1zed |SIZE=350|CAPTION= <scene name='initialview01'>1zed</scene>, resolution 1.57&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PO3:PHOSPHITE+ION'>PO3</scene> and <scene name='pdbligand=PNP:METHYL-PHOSPHONIC ACID MONO-(4-NITRO-PHENYL) ESTER'>PNP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1]
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|GENE=
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}}
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'''Alkaline phosphatase from human placenta in complex with p-nitrophenyl-phosphonate'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ZED is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=PO3:'>PO3</scene> and <scene name='pdbligand=PNP:'>PNP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZED OCA].
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1ZED is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZED OCA].
==Reference==
==Reference==
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Structural studies of human placental alkaline phosphatase in complex with functional ligands., Llinas P, Stura EA, Menez A, Kiss Z, Stigbrand T, Millan JL, Le Du MH, J Mol Biol. 2005 Jul 15;350(3):441-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15946677 15946677]
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Structural studies of human placental alkaline phosphatase in complex with functional ligands., Llinas P, Stura EA, Menez A, Kiss Z, Stigbrand T, Millan JL, Le Du MH, J Mol Biol. 2005 Jul 15;350(3):441-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15946677 15946677]
[[Category: Alkaline phosphatase]]
[[Category: Alkaline phosphatase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: substrate analog]]
[[Category: substrate analog]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:34:26 2008''

Revision as of 13:34, 20 March 2008

Image:1zed.gif


PDB ID 1zed

Drag the structure with the mouse to rotate
, resolution 1.57Å
Ligands: , , , , and
Activity: Alkaline phosphatase, with EC number 3.1.3.1
Coordinates: save as pdb, mmCIF, xml



Alkaline phosphatase from human placenta in complex with p-nitrophenyl-phosphonate


Contents

Overview

The activity of human placental alkaline phosphatase (PLAP) is downregulated by a number of effectors such as l-phenylalanine, an uncompetitive inhibitor, 5'-AMP, an antagonist of the effects of PLAP on fibroblast proliferation and by p-nitrophenyl-phosphonate (PNPPate), a non-hydrolysable substrate analogue. For the first two, such regulation may be linked to its biological function that requires a reduced and better-regulated hydrolytic rate. To understand how such disparate ligands are able to inhibit the enzyme, we solved the structure of the complexes at 1.6A, 1.9A and 1.9A resolution, respectively. These crystal structures are the first of an alkaline phosphatase in complex with organic inhibitors. Of the three inhibitors, only l-Phe and PNPPate bind at the active site hydrophobic pocket, providing structural data on the uncompetitive inhibition process. In contrast, all three ligands interact at a remote peripheral site located 28A from the active site. In order to extend these observations to the other members of the human alkaline phosphatase family, we have modelled the structures of the other human isozymes and compared them to PLAP. This comparison highlights the crucial role played by position 429 at the active site in the modulation of the catalytic process, and suggests that the peripheral binding site may be involved in the functional specialization of the PLAP isozyme.

Disease

Known disease associated with this structure: Osteoarthritis, susceptibility to OMIM:[608135]

About this Structure

1ZED is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural studies of human placental alkaline phosphatase in complex with functional ligands., Llinas P, Stura EA, Menez A, Kiss Z, Stigbrand T, Millan JL, Le Du MH, J Mol Biol. 2005 Jul 15;350(3):441-51. PMID:15946677

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