1zed: Difference between revisions

Revision as of 18:27, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1zed.png

Template:STRUCTURE 1zed

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

Template:ABSTRACT PUBMED 15946677

About this StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Sun Jul 27 18:27:13 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1zed.gif|left|200px]]
+{{Seed}}
+[[Image:1zed.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1zed|  PDB=1zed  |  SCENE=  }}
-'''Alkaline phosphatase from human placenta in complex with p-nitrophenyl-phosphonate'''
+===Alkaline phosphatase from human placenta in complex with p-nitrophenyl-phosphonate===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15946677}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15946677 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15946677}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Phosphoserine]]
 [[Category: Substrate analog]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:31:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:27:13 2008''