{'fraction_non_alphanumeric': 0.025594149908592323, 'fraction_numerical': 0.019195612431444242, 'mean_word_length': 5.257142857142857, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Integrated structural and functional model of the human ESCRT‐II complex

ESCRT‐II plays a pivotal role in receptor downregulation and multivesicular body biogenesis, and is conserved from yeast to humans. The crystal structures of two human ESCRT‐II complex structures have been determined at 2.6 and 2.9 Åresolution, respectively. The complex has three lobes and contains one copy each of VPS22 and VPS36, and two copies of VPS25. The structure reveals a dynamic helical domain to which both the VPS22 and VPS36 subunits contribute, which serves as a platform connecting the GLUE domain to the rest of the ESCRT‐II core. Hydrodynamic analysis shows that intact ESCRT‐II has a compact, closed conformation. ESCRT‐II binds to the ESCRT‐I VPS28 C‐terminal domain subunit through a helix immediately C‐terminal to the VPS36‐GLUE domain. ESCRT‐II is targeted to membranes by phosphatidylinositol 3‐phosphate binding to the GLUE domain and nonspecific polyanionic lipid binding by the first helix of VPS22. These data provide a unifying structural and functional framework for the ESCRT‐II complex.