1j2n: Difference between revisions

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[[Image:1j2n.jpg|left|200px]]<br /><applet load="1j2n" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Solution structure of CPI-17(22-120) T38D'''<br />
{{Structure
|PDB= 1j2n |SIZE=350|CAPTION= <scene name='initialview01'>1j2n</scene>
|SITE=  
|LIGAND=  
|ACTIVITY=  
|GENE=  
}}
 
'''Solution structure of CPI-17(22-120) T38D'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1J2N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2N OCA].  
1J2N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2N OCA].  


==Reference==
==Reference==
Distinctive solution conformation of phosphatase inhibitor CPI-17 substituted with aspartate at the phosphorylation-site threonine residue., Ohki S, Eto M, Shimizu M, Takada R, Brautigan DL, Kainosho M, J Mol Biol. 2003 Mar 7;326(5):1539-47. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12595264 12595264]
Distinctive solution conformation of phosphatase inhibitor CPI-17 substituted with aspartate at the phosphorylation-site threonine residue., Ohki S, Eto M, Shimizu M, Takada R, Brautigan DL, Kainosho M, J Mol Biol. 2003 Mar 7;326(5):1539-47. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12595264 12595264]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: helix bundle]]
[[Category: helix bundle]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:15 2008''
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Revision as of 12:58, 20 March 2008

File:1j2n.jpg


PDB ID 1j2n

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Solution structure of CPI-17(22-120) T38D


OverviewOverview

We present solution NMR structures for wild-type and mutated forms of CPI-17, a phosphoinhibitor for protein phosphatase 1. Phosphorylation of Thr38 of CPI-17 produces a >1000-fold increase in inhibitory potency for myosin phosphatase. We compared the 1H-15N heteronuclear single quantum coherence spectroscopy (HSQC) chemical shifts of wild-type CPI-17, partially phosphorylated CPI-17 and CPI-17 with Thr38 replaced with Asp to introduce a negative charge. There was a switch in the protein conformation due to either Asp substitution or phosphorylation, so we determined the solution NMR structure of the CPI-17 T38D mutant as a model for the active (phospho-) conformation. The structures reveal a molecular switch in conformation that involves the rotation of two of the four helices in the four helix bundle. Despite this conformational switch, there was little increase in the inhibitory potency with T38D. We propose that for this inhibitor, a negative charge at residue 38 is sufficient to trigger an active conformation, but a phosphoryl group is required for full inhibitory potency against protein phosphatase-1.

About this StructureAbout this Structure

1J2N is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

ReferenceReference

Distinctive solution conformation of phosphatase inhibitor CPI-17 substituted with aspartate at the phosphorylation-site threonine residue., Ohki S, Eto M, Shimizu M, Takada R, Brautigan DL, Kainosho M, J Mol Biol. 2003 Mar 7;326(5):1539-47. PMID:12595264

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