Differential effects of zinc binding on structured and disordered regions in the multidomain STIL protein.

ABSTRACT: Binding of metal ions is an important regulatory mechanism in proteins. Specifically, Zn²⁺ binding to disordered regions commonly induces a disorder to order transition and gain of structure or oligomerization. Here we show that simultaneous binding of Zn²⁺ ions has different effects on structured and disordered domains in the same multidomain protein. The centrosomal STIL protein bound Zn²⁺ ions via both its structured N-terminal domain (NTD) and disordered central region (IDR). Zn²⁺ binding induced structural rearrangement of the structured NTD but promoted oligomerization of the IDR. We suggest that by binding Zn²⁺ STIL acquires a different conformation, which allows its oligomerization and induces its activity. Sequence alig

SUBMITTER: Amartely H 

PROVIDER: S-EPMC6014068 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature