4mp0
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | [[4mp0]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MP0 OCA]. | + | [[4mp0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MP0 OCA]. |
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:024591642</ref><references group="xtra"/><references/> | <ref group="xtra">PMID:024591642</ref><references group="xtra"/><references/> | ||
| + | [[Category: Buffalo rat]] | ||
| + | [[Category: Human]] | ||
[[Category: Phosphoprotein phosphatase]] | [[Category: Phosphoprotein phosphatase]] | ||
[[Category: Choy, M S.]] | [[Category: Choy, M S.]] | ||
Revision as of 06:00, 23 April 2014
Contents |
Structure of a second nuclear PP1 Holoenzyme, crystal form 2
Template:ABSTRACT PUBMED 24591642
Function
[PP1A_HUMAN] Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development.[1] [PP1RA_RAT] Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers.[2] [3]
About this Structure
4mp0 is a 4 chain structure with sequence from Buffalo rat and Human. Full crystallographic information is available from OCA.
Reference
- Choy MS, Hieke M, Kumar GS, Lewis GR, Gonzalez-Dewhitt KR, Kessler RP, Stein BJ, Hessenberger M, Nairn AC, Peti W, Page R. Understanding the antagonism of retinoblastoma protein dephosphorylation by PNUTS provides insights into the PP1 regulatory code. Proc Natl Acad Sci U S A. 2014 Mar 3. PMID:24591642 doi:http://dx.doi.org/10.1073/pnas.1317395111
- ↑ Mi J, Guo C, Brautigan DL, Larner JM. Protein phosphatase-1alpha regulates centrosome splitting through Nek2. Cancer Res. 2007 Feb 1;67(3):1082-9. PMID:17283141 doi:10.1158/0008-5472.CAN-06-3071
- ↑ Allen PB, Kwon YG, Nairn AC, Greengard P. Isolation and characterization of PNUTS, a putative protein phosphatase 1 nuclear targeting subunit. J Biol Chem. 1998 Feb 13;273(7):4089-95. PMID:9461602
- ↑ Kim YM, Watanabe T, Allen PB, Kim YM, Lee SJ, Greengard P, Nairn AC, Kwon YG. PNUTS, a protein phosphatase 1 (PP1) nuclear targeting subunit. Characterization of its PP1- and RNA-binding domains and regulation by phosphorylation. J Biol Chem. 2003 Apr 18;278(16):13819-28. Epub 2003 Feb 6. PMID:12574161 doi:http://dx.doi.org/10.1074/jbc.M209621200
