Changing the topology of protein backbone: the effect of backbone cyclization on the structure and dynamics of a SH3 domain.

ABSTRACT: Understanding of the effects of the backbone cyclization on the structure and dynamics of a protein is essential for using protein topology engineering to alter protein stability and function. Here we have determined, for the first time, the structure and dynamics of the linear and various circular constructs of the N-SH3 domain from protein c-Crk. These constructs differ in the length and amino acid composition of the cyclization region. The backbone cyclization was carried out using intein-mediated intramolecular chemical ligation between the juxtaposed N- and the C-termini. The structure and backbone dynamics studies were performed using solution NMR. Our data suggest that the backbone cyclization has little effect on the overall three-dimensional structure of the SH3 domain: besides th

SUBMITTER: Schumann FH 

PROVIDER: S-EPMC4389572 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature