Protein-protein interaction

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A protein-protein interaction is an interaction between two or more proteins . It is based predominantly on non- covalent interactions, such as van der Waals forces and hydrogen bonds , electrostatic interactions and hydrophobic effects of the amino acid residues near the surface of the protein domains between the proteins involved.


Protein-protein interactions play a key role in practically all biological processes in which proteins are involved. These include in particular signal transduction processes , transport functions and the cytoskeleton . Hence, protein-protein interactions are the subject of research in many areas of life sciences . The totality of protein-protein interactions, which form a network of around 650,000 interactions in the human organism, is generally also referred to as an interactome and is registered in databases such as KEGG and Reactome . Interactions defined in the same way are e.g. B. protein-lipid interactions , protein-RNA interactions, and protein-DNA interactions .

List of methods for elucidating protein-protein interactions

Protein-protein interactions can be investigated experimentally in the course of protein characterization with the help of biochemical and biophysical methods. These include:

By comparing the amino acid sequence with databases such as BLASTp and Pfam , sequence-related proteins with known functions can give an indication of the possible functions of the protein to be examined. In addition, with the help of theoretical, computer-aided methods in the course of a protein structure prediction, the prediction of protein-protein interactions is partially possible.


Individual evidence

  1. Stump M, Thorne T, et al. : Estimating the size of the human interactome . In: PNAS . 105, No. 19, 2008, p. 6959.
  2. ^ S. Schmollinger, D. Strenkert, V. Offeddu, A. Nordhues, F. Sommer, M. Schroda: A protocol for the identification of protein-protein interactions based on 15N metabolic labeling, immunoprecipitation, quantitative mass spectrometry and affinity modulation. In: Journal of visualized experiments: JoVE. Number 67, 2012, S., doi : 10.3791 / 4083 , PMID 23051728 , PMC 3490270 (free full text).
  3. KJ Roux, DI Kim, M. Raida, B. Burke: A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells. In: Journal of Cell Biology . Volume 196, number 6, March 2012, pp. 801-810, doi : 10.1083 / jcb.201112098 , PMID 22412018 , PMC 3308701 (free full text).