{"doi":"10.1073/pnas.0902651106","title":"The eye lens chaperone α-crystallin forms defined globular assemblies","abstract":"<jats:p>α-Crystallins are molecular chaperones that protect vertebrate eye lens proteins from detrimental protein aggregation. αB-Crystallin, 1 of the 2 α-crystallin isoforms, is also associated with myopathies and neuropathological diseases. Despite the importance of α-crystallins in protein homeostasis, only little is known about their quaternary structures because of their seemingly polydisperse nature. Here, we analyzed the structures of recombinant α-crystallins using biophysical methods. In contrast to previous reports, we show that αB-crystallin assembles into defined oligomers consisting of 24 subunits. The 3-dimensional (3D) reconstruction of αB-crystallin by electron microscopy reveals a sphere-like structure with large openings to the interior of the protein. αA-Crystallin forms, in addition to complexes of 24 subunits, also smaller oligomers and large clusters consisting of individual oligomers. This propensity might explain the previously reported polydisperse nature of α-crystallin.</jats:p>","journal":"Proceedings of the National Academy of Sciences","year":2009,"id":22518,"datarank":5.386006916471758,"base_score":4.969813299576001,"endowment":4.969813299576001,"self_citation_contribution":0.7454719949364003,"citation_network_contribution":4.640534921535358,"self_endowment_contribution":0.7454719949364003,"citer_contribution":4.640534921535358,"corpus_percentile":null,"corpus_rank":null,"citation_count":143,"citer_count":124,"citers_with_citation_signal":112,"citers_with_endowment":112,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":141317,"name":"Nathalie Braun","orcid":null,"position":1,"is_corresponding":false},{"id":141318,"name":"Titus M. 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