2o8a
From Proteopedia
(New page: 200px<br /><applet load="2o8a" size="450" color="white" frame="true" align="right" spinBox="true" caption="2o8a, resolution 2.610Å" /> '''rat PP1cgamma compl...) |
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| - | [[Image:2o8a.jpg|left|200px]]<br /><applet load="2o8a" size=" | + | [[Image:2o8a.jpg|left|200px]]<br /><applet load="2o8a" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2o8a, resolution 2.610Å" /> | caption="2o8a, resolution 2.610Å" /> | ||
'''rat PP1cgamma complexed with mouse inhibitor-2'''<br /> | '''rat PP1cgamma complexed with mouse inhibitor-2'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2O8A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] Full crystallographic information is available from [http:// | + | 2O8A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O8A OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein phosphatase]] | [[Category: protein phosphatase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:56:14 2008'' |
Revision as of 10:56, 23 January 2008
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rat PP1cgamma complexed with mouse inhibitor-2
Overview
The functional specificity of type 1 protein phosphatases (PP1) depends on, the associated regulatory/targeting and inhibitory subunits. To gain, insights into the mechanism of PP1 regulation by inhibitor-2, an ancient, and intrinsically disordered regulator, we solved the crystal structure of, the complex to 2.5A resolution. Our studies show that, when complexed with, PP1c, I-2 acquires three regions of order: site 1, residues 12-17, binds, adjacent to a region recognized by many PP1 regulators; site 2, amino, acids 44-56, interacts along the RVXF binding groove through an, unsuspected sequence, KSQKW; and site 3, residues 130-169, forms, alpha-helical regions that lie across the substrate-binding cleft., Specifically, residues 148-151 interact at the catalytic center, displacing essential metal ions, accounting for both rapid inhibition and, slower inactivation of PP1c. Thus, our structure provides novel insights, into the mechanism of PP1 inhibition and subsequent reactivation, has, broad implications for the physiological regulation of PP1, and highlights, common inhibitory interactions among phosphoprotein phosphatase family, members.
About this Structure
2O8A is a Protein complex structure of sequences from Mus musculus and Rattus norvegicus. Active as Phosphoprotein phosphatase, with EC number 3.1.3.16 Full crystallographic information is available from OCA.
Reference
Structural basis for regulation of protein phosphatase 1 by inhibitor-2., Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, Depaoli-Roach AA, J Biol Chem. 2007 Sep 28;282(39):28874-83. Epub 2007 Jul 18. PMID:17636256
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