2hhm

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[[Image:2hhm.jpg|left|200px]]
[[Image:2hhm.jpg|left|200px]]
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{{Structure
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|PDB= 2hhm |SIZE=350|CAPTION= <scene name='initialview01'>2hhm</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_2hhm", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=GD:GADOLINIUM+ATOM'>GD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Inositol-phosphate_phosphatase Inositol-phosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.25 3.1.3.25] </span>
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{{STRUCTURE_2hhm| PDB=2hhm | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hhm OCA], [http://www.ebi.ac.uk/pdbsum/2hhm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hhm RCSB]</span>
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'''STRUCTURE OF INOSITOL MONOPHOSPHATASE, THE PUTATIVE TARGET OF LITHIUM THERAPY'''
'''STRUCTURE OF INOSITOL MONOPHOSPHATASE, THE PUTATIVE TARGET OF LITHIUM THERAPY'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bone, R.]]
[[Category: Bone, R.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:18:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:30:40 2008''
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Revision as of 03:18, 4 May 2008

Template:STRUCTURE 2hhm

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. 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 Sun May 4 06:18:21 2008

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