Structural Consequences of Disease-Related Mutations for Protein-Protein Interactions

Mutation of a single amino acid in a protein often has consequences on the interaction with other proteins, which may affect other interaction networks and pathways and ultimately lead to pathological phenotypes. A detailed structural analysis of these altered protein–protein complexes is essential to interpret the impact of a given mutation at the molecular level, which may facilitate intervention with therapeutic purposes. Given current limitations in the structural coverage of the human interactome, computational docking is emerging as a complementary source of information. Structural analysis can help to locate a given mutation at a protein–protein interface, but further characterisation of its impact on binding affinity is needed for a full interpretation. The integration of computational docking methods and energy‐based descriptors is facilitating the characterisation of an increasing number of disease‐related mutations, thus improving our understanding of the consequences of such mutations at the phenotypic level.

Bibliographic Details

Main Authors:	Rosell, Mireia, Fernández-Recio, Juan
Format:	capítulo de libro biblioteca
Published:	John Wiley & Sons 2020-05-16
Subjects:	Protein–protein interactions, Single amino acid variants, Structural bioinformatics, Computational docking, Interface prediction, Binding affinity change,
Online Access:	http://hdl.handle.net/10261/235838
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