Daniele Casciari

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We introduce a computational protocol for effective predictions of the supramolecular organization of integral transmembrane proteins, starting from the monomer. Despite the demonstrated constitutive and functional importance of supramolecular assemblies of transmembrane subunits or proteins, effective tools for structure predictions of such assemblies are(More)
Integrins are a family of alphabeta heterodimeric receptors essential to cell adhesion in all metazoans. In humans, the family consists of 18 alpha and 8 beta subunits that combine to form 24 dimers. Here, we present phylogenetic reconstructions for the alpha and beta integrin subunits based on sequences from 24 invertebrate and vertebrate species,(More)
A computational approach based upon rigid-body docking, ad hoc filtering, and cluster analysis has been combined with a protocol for dimerization free energy estimations to predict likely interfaces in the neurotensin 1 receptor (NTS1) homodimers. The results of this study suggest that the likely intermonomer interfaces compatible with in vitro binding(More)
In spite of the ever-increasing evidence that G protein-coupled receptors (GPCRs) form dimers/oligomers, the biological role(s) and structural architecture of homologous and heterologous receptor aggregation are, however, far from being clarified. This chapter reviews the insights gained so far, at multiscale levels of resolution, on GPCR(More)
This study represents an extension to the outer membrane phospholipase A protein (OMPLA) of the docking-based protocols previously developed for quaternary structure predictions of transmembrane oligomeric proteins and for estimating mutational effects on the thermodynamics of protein-protein and protein-DNA association. Predictions of the likely(More)
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