Interactors with experimental structures
Interactors with alphafold structures
ATG5 plays a crucial role during autophagy by facilitating the lipidation of ATG8 family proteins onto autophagosomal membranes. The crystal structure of ATG5 has revealed the presence of two ubiquitin-like-fold domains (UFDs), akin to UblA and UblB. These UFDs are separated by a helix-rich (HR) domain situated between them (PMID: 25484072). Through a ubiquitin-like conjugating system involving ATG7 (the E1-like activating enzyme) and ATG10 (E2-like conjugating enzyme), ATG5 forms a conjugate with ATG12, which is essential for its function. This ATG12-ATG5 conjugate, in conjunction with ATG16L1, acts as an E3-like enzyme, promoting the lipidation of ATG8 family proteins (PMID: 12207896, 22170153). Additionally, ATG5 is involved in various other functions, such as mitochondrial quality control following oxidative damage, negative regulation of the innate antiviral immune response. It functions in lymphocyte development and proliferation, MHC II antigen presentation, adipocyte differentiation, and apoptosis (PMID: 22247332).
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