Structure of the SLy1 SAM homodimer reveals a new interface for SAM domain self-association.

ABSTRACT: Sterile alpha motif (SAM) domains are protein interaction modules that are involved in a diverse range of biological functions such as transcriptional and translational regulation, cellular signalling, and regulation of developmental processes. SH3 domain-containing protein expressed in lymphocytes 1 (SLy1) is involved in immune regulation and contains a SAM domain of unknown function. In this report, the structure of the SLy1 SAM domain was solved and revealed that this SAM domain forms a symmetric homodimer through a novel interface. The interface consists primarily of the two long C-terminal helices, α5 and α5', of the domains packing against each other. The dimerization is characterized by a dissociation constant in the lower micromolar range. A SLy1 SAM domain construct with an extend

SUBMITTER: Kukuk L 

PROVIDER: S-EPMC6328559 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature