title: Transient protein-protein interactions.
abstract: Transient complexes are crucial for diverse biological processes such as biochemical pathways and signaling cascades in the cell. Here, we give an overview of the transient interactions; the importance of transient interactions as drug targets; and the structural characterization of transient protein-protein complexes based on the geometrical and physicochemical features of the transient complexes' interfaces. To better understand and eventually design transient protein-protein interactions (TPPIs), a molecular perspective of the protein-protein interfaces is necessary. Obtaining high-quality structures of protein-protein interactions could be one way of achieving this goal. After introducing the association kinetics of TPPIs, we elaborate on the experimental techniques detecting TPPIs in combination with the computational methods which classify transient and/or non-obligate complexes. In this review, currently available databases and servers that can be used to identify and predict TPPIs are also compiled.
authors.affiliation: Center for Computational Biology and Bioinformatics, College of Engineering, Koc University, Istanbul, Turkey.
authors.forename: Saliha Ece
authors.initials: SE
authors.lastname: Acuner Ozbabacan
authors.forename: Hatice Billur
authors.initials: HB
authors.lastname: Engin
authors.forename: Attila
authors.initials: A
authors.lastname: Gursoy
authors.forename: Ozlem
authors.initials: O
authors.lastname: Keskin
mesh_terms: D030562:Databases, Protein; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D054730:Protein Interaction Domains and Motifs; D025941:Protein Interaction Mapping; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D011506:Proteins