Signals: tinkering with domains.
Evolution reuses established modules. At the level of cell signaling, protein domains are used in many contexts to transfer different messages. A frequently occurring binding domain uses a structural scaffold to allow for sequence variation at critical sites without compromising structural stability. Even random mutations have a high chance of conferring a novel function, and only a small fraction of available sequence space is actually explored. Accordingly, current lab techniques allow us to infer evolutionary routes, exploring the possible and the attainable in terms of complex structure-function relationships.
Bornberg-Bauer
Erich
E
Institute for Evolution and Biodiversity, University of Münster, Hüfferstrasse 1, D48149, Münster, Germany. ebb@uni-muenster.de
D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry* / Q000235:genetics*; D000818:Animals; D001665:Binding Sites; D019020:Directed Molecular Evolution; D019143:Evolution, Molecular; D006801:Humans; D008024:Ligands; D016296:Mutagenesis; D009154:Mutation; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D015398:Signal Transduction / Q000502:physiology*; D013329:Structure-Activity Relationship
D048868:Adaptor Proteins, Signal Transducing; D008024:Ligands