7y4s | pdb_00007y4s
Structure of human MG53 homo-dimer
Structural highlights
FunctionTRI72_HUMAN Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity). Publication Abstract from PubMedMG53 is a tripartite motif (TRIM) family E3 ligase and plays important biological functions. Here we present the cryo-EM structure of human MG53, showing that MG53 is a homodimer consisting of a 'body' and two 'wings'. Intermolecular interactions are mainly distributed in the 'body' which is relatively stable, while two 'wings' are more dynamic. The overall architecture of MG53 is distinct from those of TRIM20 and TRIM25, illustrating the broad structural diversity of this protein family. Cryo-EM structure of human MG53 homodimer.,Niu Y, Chen G, Lv F, Xiao RP, Hu X, Chen L Biochem J. 2022 Sep 16;479(17):1909-1916. doi: 10.1042/BCJ20220385. PMID:36053137[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||
