Related ArticlesMolecular basis of the PED/PEA15 interaction with the C-terminal fragment of Phospholipase D1 revealed by NMR spectroscopy.
Biochim Biophys Acta. 2013 Apr 19;
Authors: Farina B, Doti N, Pirone L, Malgieri G, Pedone EM, Ruvo M, Fattorusso R
Abstract
PED/PEA15 is a small protein involved in many protein-protein interactions that modulates the function of a number of key cellular effectors involved in major cell functions, including apoptosis, proliferation and glucose metabolism. In particular, PED/PEA15 interacts with the phospholipase D (PLD) isoforms 1 and 2 increasing protein kinase C-? isoform activity and affects both insulin-stimulated glucose transport and glucose-stimulated insulin secretion. The C-terminal portion (residues 712-1074) of PLD1, named D4, is still able to interact with PED/PEA15. In this study we characterized, by means of NMR spectroscopy, the molecular interaction of PED/PEA15 with D4?, a smaller region of D4, encompassing residues 712-818, shown to have the same affinity for PED/PEA15 and to induce the same effects as D4 in PED/PEA15-overexpressing cells. Chemical shift perturbation (CSP) studies allowed to define D4? binding site of PED/PEA15 and to identify a smaller region likely affected by an allosteric effect. Moreover, ELISA-like experiments showed that three 20-mer overlapping synthetic peptides, covering the 762-801 region of D4?, strongly inhibit PED/PEA15-D4? interaction through their binding to PED/PEA15 with KDs in low micromolar range. Finally, molecular details of the interaction of PED/PEA15 with one of the three peptides have been revealed by CSP and saturation transfer difference (STD) analyses.
PMID: 23608947 [PubMed - as supplied by publisher]
A General Method for Constructing Atomic-ResolutionRNA Ensembles using NMR Residual Dipolar Couplings: The Basis forInterhelical Motions Revealed
A General Method for Constructing Atomic-ResolutionRNA Ensembles using NMR Residual Dipolar Couplings: The Basis forInterhelical Motions Revealed
Loi?c Salmon, Gavin Bascom, Ioan Andricioaei and Hashim M. Al-Hashimi
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja400920w/aop/images/medium/ja-2013-00920w_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja400920w
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/hvS4n8AO9ys
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[NMR paper] A General Method for Constructing Atomic-Resolution RNA Ensembles using NMR Residual Dipolar Couplings: The Basis for Inter-helical Motions Revealed.
A General Method for Constructing Atomic-Resolution RNA Ensembles using NMR Residual Dipolar Couplings: The Basis for Inter-helical Motions Revealed.
Related Articles A General Method for Constructing Atomic-Resolution RNA Ensembles using NMR Residual Dipolar Couplings: The Basis for Inter-helical Motions Revealed.
J Am Chem Soc. 2013 Mar 8;
Authors: Salmon L, Bascom GD, Andricioaei I, Al-Hashimi HM
Abstract
The ability to modulate alignment and measure multiple independent sets of NMR residual dipolar couplings (RDCs) has made it possible...
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03-12-2013 07:09 PM
Interaction of a putative BH3 domain of clusterin with anti-apoptotic Bcl-2 family proteins as revealed by NMR spectroscopy.
Interaction of a putative BH3 domain of clusterin with anti-apoptotic Bcl-2 family proteins as revealed by NMR spectroscopy.
Interaction of a putative BH3 domain of clusterin with anti-apoptotic Bcl-2 family proteins as revealed by NMR spectroscopy.
Biochem Biophys Res Commun. 2011 Apr 19;
Authors: Lee DH, Ha JH, Kim Y, Bae KH, Park JY, Choi WS, Yoon HS, Park SG, Park BC, Yi GS, Chi SW
Clusterin (CLU) is a multifunctional glycoprotein that is overexpressed in prostate and breast cancers. Although CLU is known to be involved in the regulation...
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[NMR paper] Structural preordering in the N-terminal region of ribosomal protein S4 revealed by h
Structural preordering in the N-terminal region of ribosomal protein S4 revealed by heteronuclear NMR spectroscopy.
Related Articles Structural preordering in the N-terminal region of ribosomal protein S4 revealed by heteronuclear NMR spectroscopy.
Biochemistry. 2000 Nov 7;39(44):13602-13
Authors: Sayers EW, Gerstner RB, Draper DE, Torchia DA
Protein S4, a component of the 30S subunit of the prokaryotic ribosome, is one of the first proteins to interact with rRNA in the process of ribosome assembly and is known to be involved in the regulation...
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Molecular basis of photochromism of a fluorescent protein revealed by direct 13C dete
Molecular basis of photochromism of a fluorescent protein revealed by direct 13C detection under laser illumination
Abstract Dronpa is a green fluorescent protein homologue with a photochromic property. A green laser illumination reversibly converts Dronpa from a green-emissive bright state to a non-emissive dark state, and ultraviolet illumination converts it to the bright state. We have employed solution NMR to understand the underlying molecular mechanism of the photochromism. The detail characterization of Dronpa is hindered as it is metastable in the dark state and spontaneously...
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[NMR paper] Helix formation by the phospholipase A2 38-59 fragment: influence of chain shortening
Helix formation by the phospholipase A2 38-59 fragment: influence of chain shortening and dimerization monitored by nmr chemical shifts.
Related Articles Helix formation by the phospholipase A2 38-59 fragment: influence of chain shortening and dimerization monitored by nmr chemical shifts.
Biopolymers. 1994 May;34(5):647-61
Authors: Jiménez MA, Carreño C, Andreu D, Blanco FJ, Herranz J, Rico M, Nieto JL
The solution structure of a peptide fragment corresponding to the 38-59 region of porcine phospholipase A2 has been investigated using CD,...
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[NMR paper] Helix formation by the phospholipase A2 38-59 fragment: influence of chain shortening
Helix formation by the phospholipase A2 38-59 fragment: influence of chain shortening and dimerization monitored by nmr chemical shifts.
Related Articles Helix formation by the phospholipase A2 38-59 fragment: influence of chain shortening and dimerization monitored by nmr chemical shifts.
Biopolymers. 1994 May;34(5):647-61
Authors: Jiménez MA, Carreño C, Andreu D, Blanco FJ, Herranz J, Rico M, Nieto JL
The solution structure of a peptide fragment corresponding to the 38-59 region of porcine phospholipase A2 has been investigated using CD,...
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08-22-2010 03:33 AM
[NMR paper] The molecular basis for protein kinase A anchoring revealed by solution NMR.
The molecular basis for protein kinase A anchoring revealed by solution NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nsb.gif Related Articles The molecular basis for protein kinase A anchoring revealed by solution NMR.
Nat Struct Biol. 1999 Mar;6(3):222-7
Authors: Newlon MG, Roy M, Morikis D, Hausken ZE, Coghlan V, Scott JD, Jennings PA
Compartmentalization of signal transduction enzymes into signaling complexes is an important mechanism to ensure the specificity of intracellular events. Formation of...
Molecular basis of the PED/PEA15 interaction with the C-terminal fragment of Phospholipase D1 revealed by NMR spectroscopy.
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