2bcd: Difference between revisions

Revision as of 21:14, 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:2bcd.png

Template:STRUCTURE 2bcd

X-ray crystal structure of Protein Phosphatase-1 with the marine toxin motuporin boundX-ray crystal structure of Protein Phosphatase-1 with the marine toxin motuporin bound

Template:ABSTRACT PUBMED 16343532

About this StructureAbout this Structure

2BCD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of protein phosphatase-1 bound to motuporin and dihydromicrocystin-LA: elucidation of the mechanism of enzyme inhibition by cyanobacterial toxins., Maynes JT, Luu HA, Cherney MM, Andersen RJ, Williams D, Holmes CF, James MN, J Mol Biol. 2006 Feb 10;356(1):111-20. Epub 2005 Nov 22. PMID:16343532

Page seeded by OCA on Sun Jul 27 21:14:45 2008

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

OCA

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-'''X-ray crystal structure of Protein Phosphatase-1 with the marine toxin motuporin bound'''
+===X-ray crystal structure of Protein Phosphatase-1 with the marine toxin motuporin bound===
-==Overview==
+<!--
-The microcystins and nodularins are tumour promoting hepatotoxins that are responsible for global adverse human health effects and wildlife fatalities in countries where drinking water supplies contain cyanobacteria. The toxins function by inhibiting broad specificity Ser/Thr protein phosphatases in the host cells, thereby disrupting signal transduction pathways. A previous crystal structure of a microcystin bound to the catalytic subunit of protein phosphatase-1 (PP-1c) showed distinct changes in the active site region when compared with protein phosphatase-1 structures bound to other toxins. We have elucidated the crystal structures of the cyanotoxins, motuporin (nodularin-V) and dihydromicrocystin-LA bound to human protein phosphatase-1c (gamma isoform). The atomic structures of these complexes reveal the structural basis for inhibition of protein phosphatases by these toxins. Comparisons of the structures of the cyanobacterial toxin:phosphatase complexes explain the biochemical mechanism by which microcystins but not nodularins permanently modify their protein phosphatase targets by covalent addition to an active site cysteine residue.
+The line below this paragraph, {{ABSTRACT_PUBMED_16343532}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16343532 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16343532}}
 ==About this Structure==
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 [[Category: Nodularin]]
 [[Category: Protein phosphtase]]
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