Ontology highlight
ABSTRACT:
SUBMITTER: Rimsa V
PROVIDER: S-EPMC3855715 | biostudies-literature | 2013 Dec
REPOSITORIES: biostudies-literature
Rimsa Vadim V Eadsforth Thomas C TC Hunter William N WN
Acta crystallographica. Section F, Structural biology and crystallization communications 20131128 Pt 12
Siah1 is an E3 ubiquitin ligase that contributes to proteasome-mediated degradation of multiple targets in key cellular processes and which shows promise as a therapeutic target in oncology. Structures of a truncated Siah1 bound to peptide-based inhibitors have been reported. Here, new crystallization conditions have allowed the determination of a construct encompassing dual zinc-finger subdomains and substrate-binding domains at significantly higher resolution. Although the crystals appear isom ...[more]