title: DOMMINO 2.0: integrating structurally resolved protein-, RNA-, and DNA-mediated macromolecular interactions.
abstract: Macromolecular interactions are formed between proteins, DNA and RNA molecules. Being a principle building block in macromolecular assemblies and pathways, the interactions underlie most of cellular functions. Malfunctioning of macromolecular interactions is also linked to a number of diseases. Structural knowledge of the macromolecular interaction allows one to understand the interaction's mechanism, determine its functional implications and characterize the effects of genetic variations, such as single nucleotide polymorphisms, on the interaction. Unfortunately, until now the interactions mediated by different types of macromolecules, e.g. protein-protein interactions or protein-DNA interactions, are collected into individual and unrelated structural databases. This presents a significant obstacle in the analysis of macromolecular interactions. For instance, the homogeneous structural interaction databases prevent scientists from studying structural interactions of different types but occurring in the same macromolecular complex. Here, we introduce DOMMINO 2.0, a structural Database Of Macro-Molecular INteractiOns. Compared to DOMMINO 1.0, a comprehensive database on protein-protein interactions, DOMMINO 2.0 includes the interactions between all three basic types of macromolecules extracted from PDB files. DOMMINO 2.0 is automatically updated on a weekly basis. It currently includes ∼1,040,000 interactions between two polypeptide subunits (e.g. domains, peptides, termini and interdomain linkers), ∼43,000 RNA-mediated interactions, and ∼12,000 DNA-mediated interactions. All protein structures in the database are annotated using SCOP and SUPERFAMILY family annotation. As a result, protein-mediated interactions involving protein domains, interdomain linkers, C- and N- termini, and peptides are identified. Our database provides an intuitive web interface, allowing one to investigate interactions at three different resolution levels: whole subunit network, binary interaction and interaction interface. Database URL: http://dommino.org.
authors.affiliation: Informatics Institute, University of Missouri, Columbia, MO, USA.
authors.forename: Xingyan
authors.initials: X
authors.lastname: Kuang
authors.affiliation: Department of Computer Science and Bioinformatics and Computational Biology Program, Worcester Polytechnic Institute, Worcester, MA, USA.
authors.forename: Andi
authors.initials: A
authors.lastname: Dhroso
authors.affiliation: Informatics Institute, University of Missouri, Columbia, MO, USA.
authors.forename: Jing Ginger
authors.initials: JG
authors.lastname: Han
authors.affiliation: Informatics Institute, University of Missouri, Columbia, MO, USA, Department of Electrical and Computer Engineering, Department of Computer Science, University of Missouri, Columbia, MO, USA.
authors.forename: Chi-Ren
authors.initials: CR
authors.lastname: Shyu
authors.affiliation: Department of Computer Science and Bioinformatics and Computational Biology Program, Worcester Polytechnic Institute, Worcester, MA, USA, korkin@korkinlab.org.
authors.forename: Dmitry
authors.initials: D
authors.lastname: Korkin
mesh_terms: D019295:Computational Biology / Q000379:methods*; D003198:Computer Simulation; D004247:DNA / Q000737:chemistry*; D030562:Databases, Protein; D014644:Genetic Variation; D006801:Humans; D020407:Internet; D046911:Macromolecular Substances / Q000737:chemistry*; D020641:Polymorphism, Single Nucleotide; D025941:Protein Interaction Mapping; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry; D012313:RNA / Q000737:chemistry*; D012984:Software; D014780:Viruses
chemical_list: D046911:Macromolecular Substances; D011506:Proteins; D012313:RNA; D004247:DNA
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