1j2m
From Proteopedia
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| - | [[Image:1j2m.jpg|left|200px]] | + | [[Image:1j2m.jpg|left|200px]] |
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| - | '''Solution structure of CPI-17(22-120)''' | + | {{Structure |
| + | |PDB= 1j2m |SIZE=350|CAPTION= <scene name='initialview01'>1j2m</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution structure of CPI-17(22-120)''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1J2M is a [ | + | 1J2M 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=1J2M 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:// | + | 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 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:58:03 2008'' |
Revision as of 09:58, 20 March 2008
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Solution structure of CPI-17(22-120)
Overview
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 Structure
1J2M is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
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:12595264
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