2hhm
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="2hhm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hhm, resolution 2.1Å" /> '''STRUCTURE OF INOSITO...)
Next diff →
Revision as of 20:26, 12 November 2007
|
STRUCTURE OF INOSITOL MONOPHOSPHATASE, THE PUTATIVE TARGET OF LITHIUM THERAPY
Overview
Inositol monophosphatase (EC 3.1.3.25), the putative molecular site of, action of lithium therapy for manic-depressive illness, plays a key role, in the phosphatidylinositol signaling pathway by catalyzing the hydrolysis, of inositol monophosphates. To provide a structural basis from which to, design better therapeutic agents for manic-depressive illness, the, structure of human inositol monophosphatase has been determined to 2.1-A, resolution by using x-ray crystallography. The enzyme exists as a dimer of, identical subunits, each folded into a five-layered sandwich of three, pairs of alpha-helices and two beta-sheets. Sulfate and an inhibitory, lanthanide cation (Gd3+) are bound at identical sites on each subunit and, establish the positions of the active sites. Each site is located in a, large hydrophilic cavern that is at the base of the two central helices, where several segments of secondary structure intersect. Comparison of the, phosphatase aligned sequences of several diverse genes with the, phosphatase structure suggests that the products of these genes and the, phosphatase form a structural family with a conserved metal binding site.
About this Structure
2HHM is a Single protein structure of sequence from Homo sapiens with SO4 and GD as ligands. Active as Inositol-phosphate phosphatase, with EC number 3.1.3.25 Full crystallographic information is available from OCA.
Reference
Structure of inositol monophosphatase, the putative target of lithium therapy., Bone R, Springer JP, Atack JR, Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10031-5. PMID:1332026
Page seeded by OCA on Mon Nov 12 22:32:48 2007
