Addressing the role of the α-helical extension in the folding of the third PDZ domain from PSD-95.

ABSTRACT: PDZ domains are one of the most important protein-protein interaction domains in human. While presenting a conserved three dimensional structure, a substantial number of PDZ domains display structural extensions suggested to be involved in their folding and binding mechanisms. The C-terminal α-helix extension (α3) of the third PDZ domain from PSD-95 (PDZ3) has been reported to have a role in function of the domain as well as in the stabilization of the native fold. Here we report an evaluation of the effect of the truncation of this additional helix on the folding and unfolding kinetics of PDZ3. Fluorescent variants of full length and truncated PDZ3 were produced and stopped-flow fluorescence measurements were made under different experimental conditions (pH, ionic strength and temperature

SUBMITTER: Gautier C 

PROVIDER: S-EPMC5626748 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature