Related ArticlesSolution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosphorylation-induced conformational changes responsible for activation.
J Mol Biol. 2001 Dec 7;314(4):839-49
Authors: Ohki S, Eto M, Kariya E, Hayano T, Hayashi Y, Yazawa M, Brautigan D, Kainosho M
Contractility of vascular smooth muscle depends on phosphorylation of myosin light chains, and is modulated by hormonal control of myosin phosphatase activity. Signaling pathways activate kinases such as PKC or Rho-dependent kinases that phosphorylate the myosin phosphatase inhibitor protein called CPI-17. Phosphorylation of CPI-17 at Thr38 enhances its inhibitory potency 1000-fold, creating a molecular on/off switch for regulating contraction. We report the solution NMR structure of the CPI-17 inhibitory domain (residues 35-120), which retains the signature biological properties of the full-length protein. The final ensemble of 20 sets of NMR coordinates overlaid onto their mean structure with r.m.s.d. values of 0.84(+/-0.22) A for the backbone atoms. The protein forms a novel four-helix, V-shaped bundle comprised of a central anti-parallel helix pair (B/C helices) flanked by two large spiral loops formed by the N and C termini that are held together by another anti-parallel helix pair (A/D helices) stabilized by intercalated aromatic and aliphatic side-chains. Chemical shift perturbations indicated that phosphorylation of Thr38 induces a conformational change involving displacement of helix A, without significant movement of the other three helices. This conformational change seems to flex one arm of the molecule, thereby exposing new surfaces of the helix A and the nearby phosphorylation loop to form specific interactions with the catalytic site of the phosphatase. This phosphorylation-dependent conformational change offers new structural insights toward understanding the specificity of CPI-17 for myosin phosphatase and its function as a molecular switch.
[NMR paper] NMR solution structure of ATTp, an Arabidopsis thaliana trypsin inhibitor.
NMR solution structure of ATTp, an Arabidopsis thaliana trypsin inhibitor.
Related Articles NMR solution structure of ATTp, an Arabidopsis thaliana trypsin inhibitor.
Biochemistry. 2002 Oct 15;41(41):12284-96
Authors: Zhao Q, Chae YK, Markley JL
The three-dimensional structure of the precursor form of the Arabidopsis thaliana trypsin inhibitor (ATT(p), GenBank entry Z46816), a 68-residue (approximately 7.5 kDa) rapeseed class proteinase inhibitor, has been determined in solution at pH 5.0 and 25 degrees C by multinuclear magnetic resonance...
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[NMR paper] NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1
NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors.
Related Articles NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors.
Protein Sci. 2000 May;9(5):976-84
Authors: Cierpicki T, Bania J, Otlewski J
The three-dimensional structure of the 56 residue polypeptide Apis mellifera chymotrypsin/cathepsin G inhibitor 1 (AMCI-1) isolated from honey bee hemolymph was...
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11-18-2010 09:15 PM
[NMR paper] The NMR structure of the 5S rRNA E-domain-protein L25 complex shows preformed and ind
The NMR structure of the 5S rRNA E-domain-protein L25 complex shows preformed and induced recognition.
Related Articles The NMR structure of the 5S rRNA E-domain-protein L25 complex shows preformed and induced recognition.
EMBO J. 1999 Nov 15;18(22):6508-21
Authors: Stoldt M, Wöhnert J, Ohlenschläger O, Görlach M, Brown LR
The structure of the complex between ribosomal protein L25 and a 37 nucleotide RNA molecule, which contains the E-loop and helix IV regions of the E-domain of Escherichia coli 5S rRNA, has been determined to an overall...
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[NMR paper] The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general
The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases.
Related Articles The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases.
EMBO J. 1998 Nov 2;17(21):6377-84
Authors: Stoldt M, Wöhnert J, Görlach M, Brown LR
The structure of the Escherichia coli ribosomal protein L25 has been determined to an r.m.s. displacement of backbone heavy atoms of 0.62 +/- 0.14 A by multi-dimensional...
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[NMR paper] Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent pro
Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics.
Related Articles Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics.
J Pept Res. 1997 Mar;49(3):210-20
Authors: Padilla A, Hauer JA, Tsigelny I, Parello J, Taylor SS
Peptides derived from the inhibitor of cAMP-dependent protein kinase. PKI, have been studied by 2D 1H NMR techniques. These include the inhibitor...
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[NMR paper] Investigation of the solution structure of chymotrypsin inhibitor 2 using molecular d
Investigation of the solution structure of chymotrypsin inhibitor 2 using molecular dynamics: comparison to x-ray crystallographic and NMR data.
Related Articles Investigation of the solution structure of chymotrypsin inhibitor 2 using molecular dynamics: comparison to x-ray crystallographic and NMR data.
Protein Eng. 1995 Nov;8(11):1117-28
Authors: Li A, Daggett V
The native solution structure and dynamics of chymotrypsin inhibitor 2 (CI2) have been studied using a long (5.3 ns) molecular dynamics (MD) simulation without any imposed...
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[NMR paper] Three-dimensional solution structure of Cucurbita maxima trypsin inhibitor-V determin
Three-dimensional solution structure of Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy.
Related Articles Three-dimensional solution structure of Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy.
Biochemistry. 1995 Apr 18;34(15):5201-11
Authors: Cai M, Gong Y, Kao JL, Krishnamoorthi R
The solution structure of Cucurbita maxima trypsin inhibitor-V (CMTI-V), which is also a specific inhibitor of the blood coagulation protein, factor XIIa, was determined by 1H NMR spectroscopy in combination with a...
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[NMR paper] The three-dimensional solution structure by 1H NMR of a 6-kDa proteinase inhibitor is
The three-dimensional solution structure by 1H NMR of a 6-kDa proteinase inhibitor isolated from the stigma of Nicotiana alata.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The three-dimensional solution structure by 1H NMR of a 6-kDa proteinase inhibitor isolated from the stigma of Nicotiana alata.
J Mol Biol. 1994 Sep 23;242(3):231-43
Authors: Nielsen KJ, Heath RL, Anderson MA, Craik DJ
The three-dimensional structure and disulfide connectivities of a 6-kDa...
Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosp
Linear Mode
