Ontology highlight
ABSTRACT:
SUBMITTER: Franke B
PROVIDER: S-EPMC3971405 | biostudies-literature | 2014 Mar
REPOSITORIES: biostudies-literature
Franke Barbara B Gasch Alexander A Rodriguez Dayté D Chami Mohamed M Khan Muzamil M MM Rudolf Rüdiger R Bibby Jaclyn J Hanashima Akira A Bogomolovas Julijus J von Castelmur Eleonore E Rigden Daniel J DJ Uson Isabel I Labeit Siegfried S Mayans Olga O
Open biology 20140326
MuRF1 is an E3 ubiquitin ligase central to muscle catabolism. It belongs to the TRIM protein family characterized by a tripartite fold of RING, B-box and coiled-coil (CC) motifs, followed by variable C-terminal domains. The CC motif is hypothesized to be responsible for domain organization in the fold as well as for high-order assembly into functional entities. But data on CC from this family that can clarify the structural significance of this motif are scarce. We have characterized the helical ...[more]