The N-terminal region of the human autophagy protein ATG16L1 contains a domain that folds into a helical structure consistent with formation of a coiled-coil.

ABSTRACT: Autophagy is a fundamental cellular process required for organelle degradation and removal of invasive pathogens. Autophagosome formation involves the recruitment of, and interaction between, multiple proteins produced from autophagy-related (ATG) genes. One of the key complexes in autophagosome formation is the ATG12-ATG5-ATG16L1 complex. ATG16L1 functions as a molecular scaffold mediating protein-protein interactions necessary for formation of the autophagosome in response to both classical and pathogen-related autophagy stimuli. The coiled-coil domain of the yeast ortholog, ATG16, exists as a homodimer both in solution and in the crystal form. The yeast and human orthologs show poor sequence identity. Here we have sought to determine the minimal boundaries of the human ATG16L1 coiled-co

SUBMITTER: Parkhouse R 

PROVIDER: S-EPMC3782427 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature