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|Title:||Transient Interactions of a Cytosolic Protein with Macromolecular and Vesicular Cosolutes: Unspecific and Specific Effects||Authors:||Ceccon, Alberto
Pérez Santero, Silvia
|Keywords:||NMR spectroscopy;data-driven docking;intracellular environment;macromolecular crowding;protein-protein interactions||Keywords Plus:||ACID-BINDING-PROTEIN;COARSE-GRAINED MODEL;MOLECULAR-DYNAMICS;LIGAND-BINDING;NMR;FLUORESCENCE;RELAXATION;COMPLEX;DOMAIN;WEAK||Mesh headings:||Hydroxysteroid Dehydrogenases;Macromolecular Substances||Secondary Mesh headings:||Binding Sites;Cytosol;Humans;Lipid Bilayers;Molecular Dynamics Simulation;Muramidase;Nuclear Magnetic Resonance, Biomolecular;Protein Interaction Domains and Motifs;Spectrometry, Fluorescence;Ubiquitin||Issue Date:||Dec-2015||Publisher:||WILEY-V C H VERLAG GMBH||Journal:||Chembiochem : a European journal of chemical biology||Abstract:||
Cytosolic proteins do not occur as isolated but are exposed to many interactions within a crowded cellular environment. We investigated the associations between a test cytosolic protein, human ileal bile acid binding protein (IBABP), and model cosolutes mimicking macromolecular and lipid membrane intracellular components. Using fluorescence spectroscopy, heteronuclear NMR, and molecular dynamics, we found that IBABP associated weakly with anionic lipid vesicles and experienced transient unspecific contacts with albumin. Localized dynamic perturbations were observed even in the case of apparent unspecific binding. IBABP and ubiquitin did not display mutually attractive forces, whereas IBABP associated specifically with lysozyme. A structural model of the IBABP-lysozyme complex was obtained by data-driven docking simulation. Presumably, all the interactions shown here contribute to modulating functional communication of a protein in its native environment.
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