We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1ew2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ew2.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ew2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ew2| PDB=1ew2 | SCENE= }}
{{STRUCTURE_1ew2| PDB=1ew2 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF A HUMAN PHOSPHATASE'''
+
===CRYSTAL STRUCTURE OF A HUMAN PHOSPHATASE===
-
==Overview==
+
<!--
-
Human placental alkaline phosphatase (PLAP) is one of three tissue-specific human APs extensively studied because of its ectopic expression in tumors. The crystal structure, determined at 1.8-A resolution, reveals that during evolution, only the overall features of the enzyme have been conserved with respect to Escherichia coli. The surface is deeply mutated with 8% residues in common, and in the active site, only residues strictly necessary to perform the catalysis have been preserved. Additional structural elements aid an understanding of the allosteric property that is specific for the mammalian enzyme (Hoylaerts, M. F., Manes, T., and Millan, J. L. (1997) J. Biol. Chem. 272, 22781-22787). Allostery is probably favored by the quality of the dimer interface, by a long N-terminal alpha-helix from one monomer that embraces the other one, and similarly by the exchange of a residue from one monomer in the active site of the other. In the neighborhood of the catalytic serine, the orientation of Glu-429, a residue unique to PLAP, and the presence of a hydrophobic pocket close to the phosphate product, account for the specific uncompetitive inhibition of PLAP by l-amino acids, consistent with the acquisition of substrate specificity. The location of the active site at the bottom of a large valley flanked by an interfacial crown-shaped domain and a domain containing an extra metal ion on the other side suggest that the substrate of PLAP could be a specific phosphorylated protein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11124260}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11124260 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11124260}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Non covalent complex]]
[[Category: Non covalent complex]]
[[Category: Phosphatase]]
[[Category: Phosphatase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:35:12 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:06:37 2008''

Revision as of 23:06, 30 June 2008

Image:1ew2.png

Template:STRUCTURE 1ew2

CRYSTAL STRUCTURE OF A HUMAN PHOSPHATASE

Template:ABSTRACT PUBMED 11124260

About this Structure

1EW2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity., Le Du MH, Stigbrand T, Taussig MJ, Menez A, Stura EA, J Biol Chem. 2001 Mar 23;276(12):9158-65. Epub 2000 Dec 20. PMID:11124260

Page seeded by OCA on Tue Jul 1 02:06:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ew2"
Personal tools