De novo design of allosterically switchable protein assemblies.

ABSTRACT: Allosteric modulation of protein function, wherein the binding of an effector to a protein triggers conformational changes at distant functional sites, plays a central part in the control of metabolism and cell signalling^1-3. There has been considerable interest in designing allosteric systems, both to gain insight into the mechanisms underlying such 'action at a distance' modulation and to create synthetic proteins whose functions can be regulated by effectors^4-7. However, emulating the subtle conformational changes distributed across many residues, characteristic of natural allosteric proteins, is a significant challenge^8,9. Here, inspired by the classic Monod-Wyman-Changeux model of cooperativity¹⁰, we investigate the de novo design of alloste

SUBMITTER: Pillai A 

PROVIDER: S-EPMC11338832 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature