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• W1986046522 abstract "Analysis of protein-ligand complexes and recognition of spatially conserved physico-chemical properties is important for the prediction of binding and function. Here, we present two webservers for multiple alignment and recognition of binding patterns shared by a set of protein structures. The first webserver, MultiBind (http://bioinfo3d.cs.tau.ac.il/MultiBind), performs multiple alignment of protein binding sites. It recognizes the common spatial chemical binding patterns even in the absence of similarity of the sequences or the folds of the compared proteins. The input to the MultiBind server is a set of protein-binding sites defined by interactions with small molecules. The output is a detailed list of the shared physico-chemical binding site properties. The second webserver, MAPPIS (http://bioinfo3d.cs.tau.ac.il/MAPPIS), aims to analyze protein-protein interactions. It performs multiple alignment of protein-protein interfaces (PPIs), which are regions of interaction between two protein molecules. MAPPIS recognizes the spatially conserved physico-chemical interactions, which often involve energetically important hot-spot residues that are crucial for protein-protein associations. The input to the MAPPIS server is a set of protein-protein complexes. The output is a detailed list of the shared interaction properties of the interfaces." @default.
• W1986046522 created "2016-06-24" @default.
• W1986046522 creator A5009285796 @default.
• W1986046522 creator A5020789964 @default.
• W1986046522 creator A5025357844 @default.
• W1986046522 creator A5030975599 @default.
• W1986046522 date "2008-05-19" @default.
• W1986046522 modified "2023-10-17" @default.
• W1986046522 title "MultiBind and MAPPIS: webservers for multiple alignment of protein 3D-binding sites and their interactions" @default.
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• W1986046522 doi "https://doi.org/10.1093/nar/gkn185" @default.
• W1986046522 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2447750" @default.
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