Ontology highlight
ABSTRACT:
SUBMITTER: Aichem A
PROVIDER: S-EPMC6102260 | biostudies-literature | 2018 Aug
REPOSITORIES: biostudies-literature
Aichem Annette A Anders Samira S Catone Nicola N Rößler Philip P Stotz Sophie S Berg Andrej A Schwab Ricarda R Scheuermann Sophia S Bialas Johanna J Schütz-Stoffregen Mira C MC Schmidtke Gunter G Peter Christine C Groettrup Marcus M Wiesner Silke S
Nature communications 20180820 1
FAT10 is a ubiquitin-like modifier that directly targets proteins for proteasomal degradation. Here, we report the high-resolution structures of the two individual ubiquitin-like domains (UBD) of FAT10 that are joined by a flexible linker. While the UBDs of FAT10 show the typical ubiquitin-fold, their surfaces are entirely different from each other and from ubiquitin explaining their unique binding specificities. Deletion of the linker abrogates FAT10-conjugation while its mutation blocks auto-F ...[more]