Ontology highlight
ABSTRACT:
SUBMITTER: Schmidt K
PROVIDER: S-EPMC5984491 | biostudies-literature | 2018 May
REPOSITORIES: biostudies-literature
Schmidt Karin K Gardill Bernd R BR Kern Alina A Kirchweger Peter P Börsch Michael M Muller Yves A YA
Proceedings of the National Academy of Sciences of the United States of America 20180514 22
The allosteric interplay between distant functional sites present in a single protein provides for one of the most important regulatory mechanisms in biological systems. While the design of ligand-binding sites into proteins remains challenging, this holds even truer for the coupling of a newly engineered binding site to an allosteric mechanism that regulates the ligand affinity. Here it is shown how computational design algorithms enabled the introduction of doxycycline- and doxorubicin-binding ...[more]