RT Journal Article
SR Electronic
T1 SKEMPI 2.0: An updated benchmark of changes in protein-protein binding energy, kinetics and thermodynamics upon mutation
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 341735
DO 10.1101/341735
A1 Justina Jankauskaitė
A1 Brian Jiménez-García
A1 Justas Dapkūnas
A1 Juan Fernández-Recio
A1 Iain H. Moal
YR 2018
UL http://biorxiv.org/content/early/2018/06/07/341735.abstract
AB Motivation Understanding the relationship between the sequence, structure, binding energy, binding kinetics and binding thermodynamics of protein-protein interactions is crucial to understanding cellular signaling, the assembly and regulation of molecular complexes, the mechanisms through which mutations lead to disease, and protein engineering.Results We present SKEMPI 2.0, a major update to our database of binding free energy changes upon mutation for structurally resolved protein-protein interactions. This version now contains manually curated binding data for 7085 mutations, an increase of 133%, including changes in kinetics for 1844 mutations, enthalpy and entropy changes for 443 mutations, and 440 mutations which abolish detectable binding.Availability The database is available at https://life.bsc.es/pid/skempi2/