Atomic resolution protein allostery from the multi-state structure of a PDZ domain.

ABSTRACT: Recent methodological advances in solution NMR allow the determination of multi-state protein structures and provide insights into structurally and dynamically correlated protein sites at atomic resolution. This is demonstrated in the present work for the well-studied PDZ2 domain of protein human tyrosine phosphatase 1E for which protein allostery had been predicted. Two-state protein structures were calculated for both the free form and in complex with the RA-GEF2 peptide using the exact nuclear Overhauser effect (eNOE) method. In the apo protein, an allosteric conformational selection step comprising almost 60% of the domain was detected with an "open" ligand welcoming state and a "closed" state that obstructs the binding site by changing the distance between the β-sheet 2, α-helix 2, an

SUBMITTER: Ashkinadze D 

PROVIDER: S-EPMC9584909 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature