| pubmed-article:7500362 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7500362 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:7500362 | lifeskim:mentions | umls-concept:C1956003 | lld:lifeskim |
| pubmed-article:7500362 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:7500362 | lifeskim:mentions | umls-concept:C0600499 | lld:lifeskim |
| pubmed-article:7500362 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:7500362 | lifeskim:mentions | umls-concept:C0077513 | lld:lifeskim |
| pubmed-article:7500362 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:7500362 | pubmed:dateCreated | 1996-1-18 | lld:pubmed |
| pubmed-article:7500362 | pubmed:abstractText | Protein phosphatase 1 (PP1) is a serine/threonine protein phosphatase that is essential in regulating diverse cellular processes. Here we report the crystal structure of the catalytic subunit of human PP1 gamma 1 and its complex with tungstate at 2.5 A resolution. The anomalous scattering from tungstate was used in a multiple wavelength anomalous dispersion experiment to derive crystallographic phase information. The protein adopts a single domain with a novel fold, distinct from that of the protein tyrosine phosphatases. A di-nuclear ion centre consisting of Mn2+ and Fe2+ is situated at the catalytic site that binds the phosphate moiety of the substrate. Proton-induced X-ray emission spectroscopy was used to identify the nature of the ions bound to the enzyme. The structural data indicate that dephosphorylation is catalysed in a single step by a metal-activated water molecule. This contrasts with other phosphatases, including protein tyrosine phosphatases, acid and alkaline phosphatases which form phosphoryl-enzyme intermediates. The structure of PP1 provides insight into the molecular mechanism for substrate recognition, enzyme regulation and inhibition of this enzyme by toxins and tumour promoters and a basis for understanding the expanding family of related phosphatases which include PP2A and PP2B (calcineurin). | lld:pubmed |
| pubmed-article:7500362 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7500362 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7500362 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7500362 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7500362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7500362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7500362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7500362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7500362 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7500362 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:7500362 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:7500362 | pubmed:author | pubmed-author:CohenP TPT | lld:pubmed |
| pubmed-article:7500362 | pubmed:author | pubmed-author:BarfordDD | lld:pubmed |
| pubmed-article:7500362 | pubmed:author | pubmed-author:ReinemerPP | lld:pubmed |
| pubmed-article:7500362 | pubmed:author | pubmed-author:EgloffM PMP | lld:pubmed |
| pubmed-article:7500362 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7500362 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:7500362 | pubmed:volume | 254 | lld:pubmed |
| pubmed-article:7500362 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7500362 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7500362 | pubmed:pagination | 942-59 | lld:pubmed |
| pubmed-article:7500362 | pubmed:dateRevised | 2009-9-29 | lld:pubmed |
| pubmed-article:7500362 | pubmed:meshHeading | pubmed-meshheading:7500362-... | lld:pubmed |
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| pubmed-article:7500362 | pubmed:meshHeading | pubmed-meshheading:7500362-... | lld:pubmed |
| pubmed-article:7500362 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7500362 | pubmed:articleTitle | Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. | lld:pubmed |
| pubmed-article:7500362 | pubmed:affiliation | Laboratory of Molecular Biophysics, University of Oxford, United Kingdom. | lld:pubmed |
| pubmed-article:7500362 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7500362 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| literatureCitation:2639_750... | literatureCitation:pubmed | pubmed-article:7500362 | lld:drugbank |
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