NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
FEBS J. 2010 Sep 3;
Authors: Farina B, Pirone L, Russo L, Viparelli F, Doti N, Pedone C, Pedone EM, Fattorusso R
PED/PEA-15 (phosphoprotein enriched in diabetes/phosphoprotein enriched in astrocytes) is a ubiquitously expressed protein and a key regulator of cell growth and glucose metabolism. PED/PEA-15 mediates both homotypic and heterotypic interactions and is constituted by an N-terminal canonical death effector domain and a C-terminal tail. In the present study, the backbone dynamics of PED/PEA-15 via (15)N R(1) and R(2) and steady-state [(1)H]-(15)N NOE measurements is reported. The dynamic parameters were analyzed using both Lipari-Szabo model-free formalism and a reduced spectral density mapping approach. The results obtained define a polar and charged surface of the death effector domain characterized by internal motions in the micro- to millisecond timescale, which is crucial for the multiple heterotypic functional protein-protein interactions in which PED/PEA-15 is involved. The present study contributes to a better understanding of the molecular basis of the PED/PEA-15 functional interactions and provides a more detailed surface for the design and development of PED/PEA-15 binders.
PMID: 20825483 [PubMed - as supplied by publisher]
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
Recent Developments in (15)N NMR Relaxation Studies that Probe Protein Backbone Dynamics.
Top Curr Chem. 2011 Sep 7;
Authors: Ishima R
Abstract
Nuclear Magnetic Resonance (NMR) relaxation is a powerful technique that provides information about internal dynamics associated with configurational energetics in proteins, as well as site-specific information involved in conformational equilibria. In particular, (15)N relaxation is a useful probe to...
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Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G
Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G
Abstract We performed density functional calculations of backbone 15N shielding tensors in the regions of beta-sheet and turns of protein G. The calculations were carried out for all twenty-four beta-sheet residues and eight beta-turn residues in the protein GB3 and the results were compared with the available experimental data from solid-state and solution NMR measurements. Together with the alpha-helix data, our calculations cover 39 out of the 55 residues (or 71%) in GB3....
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11-24-2010 09:01 PM
[NMR paper] NMR studies of the backbone flexibility and structure of human growth hormone: a comp
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Comparison of fast backbone dynamics at amide nitrogen and carbonyl sites in dematin
Abstract We perform a detailed comparison of fast backbone dynamics probed at amide nitrogen versus carbonyl carbon sites for dematin headpiece C-terminal domain (DHP) and its S74E mutant (DHPS74E). Carbonyl dynamics is probed via auto-correlated longitudinal rates and transverse Cā?²/Cā?²-CĪ± CSA/dipolar and Cā?²/Cā?²ā??N CSA/dipolar cross-correlated rates, while 15N data are taken from a previous study. Resulting values of effective order parameters and internal correlation times support the conclusion that Cā?² relaxation reports on a different subset of fast motions compared to those...
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
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