Cd And Nmr Conformational Studies Of A Peptide Encompassing The Mid Loop Interface Of Ship2-Sam(349 views) Mercurio FA, Scognamiglio PL, Di Natale C, Marasco D, Pellecchia M, Leone M
Keywords: Nmr, Peptide, Sam Domain, Ship2, Binding Energy, Ethanol, Neurodegenerative Diseases, Nuclear Magnetic Resonance, 2-Trifluoroethanol, Conformational Study, Helical Conformation, Structural Insights, Therapeutic Application, Ephrin Receptor A2, Phosphatase, Phosphatidylinositol 3 Kinase, Protein Derivative, Protein Sam, Protein Ship2, Unclassified Drug, Alpha Helix, Article, Circular Dichroism, Conformational Transition, Molecular Docking, Molecular Model, Protein Binding, Protein Conformation, Protein Domain, Protein Protein Interaction, Protein Structure, Buffers, Humans, Inositol Polyphosphate 5-Phosphatases, Magnetic Resonance Spectroscopy, Molecular Dynamics Simulation, Chemistry, Phosphoric Monoester Hydrolases, Secondary, Tertiary, Solutions,
Affiliations: *** IBB - CNR ***
Institute of Biostructures and Bioimaging (CNR), Naples, Italy
Department of Pharmacy, University Federico II, Naples, Italy
Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), Naples, Italy
IIT Italian Institute of Technology, Naples, Italy
Sanford-Burnham Medical Research Institute, San Diego, CA, United States
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Cd And Nmr Conformational Studies Of A Peptide Encompassing The Mid Loop Interface Of Ship2-Sam
The lipid phosphatase Ship2 is a protein that intervenes in several diseases such as diabetes, cancer, neurodegeneration, and atherosclerosis. It is made up of a catalytic domain and several protein docking modules such as a C-terminal Sam (Sterile alpha motif) domain. The Sam domain of Ship2 (Ship2-Sam) binds to the Sam domains of the EphA2 receptor (EphA2-Sam) and the PI3K effector protein Arap3 (Arap3-Sam). These heterotypic Sam-Sam interactions occur through formation of dimers presenting the canonical "Mid Loop/End Helix" binding mode. The central region of Ship2-Sam, spanning the C-terminal end of 2, the 3 and 4 helices together with the 2 3 and 3 4 interhelical loops, forms the Mid Loop surface that is needed to bind partners Sam domains. A peptide encompassing most of the Ship2-Sam Mid Loop interface (Shiptide) capable of binding to both EphA2-Sam and Arap3-Sam, was previously identified. Here we investigated the conformational features of this peptide, through solution CD and NMR studies in different conditions. These studies reveal that the peptide is highly flexible in aqueous buffer, while it adopts a helical conformation in presence of 2, 2, 2-trifluoroethanol. The discovered structural insights and in particular the identification of a helical motif, may lead to the design of more constrained and possibly cell permeable Shiptide analogs that could work as efficient antagonists of Ship2-Sam heterotypic interactions and embrace therapeutic applications. 2014 Wiley Periodicals, Inc. Biopolymers 101: 1088-1098, 2014. 2014 Wiley Periodicals, Inc
Cd And Nmr Conformational Studies Of A Peptide Encompassing The Mid Loop Interface Of Ship2-Sam
Antonini A, Vitale C, Barone P, Cilia R, Righini A, Bonuccelli U, Abbruzzese G, Ramat S, Petrone A, Quatrale R, Marconi R, Ceravolo R, Stefani A, Lopiano L, Zappia M, Capus L, Morgante L, Tamma F, Tinazzi M, Colosimo C, Guerra UP, Valzania F, Fagioli G, Distefano A, Bagnato A, Feggi L, Anna S, Maria Teresa Rosaria De Cr, Nobili F, Mazzuca N, Baldari S, Eleopra R, Bestetti A, Benti R, Varrone A, Volterrani D, Massa R, Stocchi F, Schillaci O, Dore F, Zibetti M, Castellano G, Battista SG, Giorgetti G * The relationship between cerebral vascular disease and parkinsonism: The VADO study(498 views) Parkinsonism Relat D (ISSN: 1353-8020, 1873-5126, 1873-5126electronic), 2012; 18(6): 775-780. Impact Factor:3.274 ViewExport to BibTeXExport to EndNote
Hesse B, Tagil K, Cuocolo A, Anagnostopoulos C, Bardies M, Bax J, Bengel F, Busemann Sokole E, Davies G, Dondi M, Edenbrandt L, Franken P, Kjaer A, Knuuti J, Lassmann M, Ljungberg M, Marcassa C, Marie PY, Mckiddie F, O'connor M, Prvuolovich E, Underwood R * 3. 0 T perfusion MR imaging(730 views) Rivista Di Neuroradiologia (ISSN: 1120-9976), 2004; 17(6): 807-812. Impact Factor:0.023 ViewExport to BibTeXExport to EndNote