{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Richards MW"],"funding":["Cancer Research UK","Science and Technology Facilities Council","Wellcome Trust"],"pagination":["5195-200"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3986153"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["111(14)"],"pubmed_abstract":["Proteins of the echinoderm microtubule-associated protein (EMAP)-like (EML) family contribute to formation of the mitotic spindle and interphase microtubule network. They contain a unique hydrophobic EML protein (HELP) motif and a variable number of WD40 repeats. Recurrent gene rearrangements in nonsmall cell lung cancer fuse EML4 to anaplastic lymphoma kinase (ALK), causing expression of several fusion oncoprotein variants. We have determined a 2.6-Å crystal structure of the representative ∼70-kDa core of EML1, revealing an intimately associated pair of β-propellers, which we term a TAPE (tandem atypical propeller in EMLs) domain. One propeller is highly atypical, having a discontinuous subdomain unrelated to a WD40 motif in place of one of its blades. This unexpected feature shows how a "],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Crystal structure of EML1 reveals the basis for Hsp90 dependence of oncogenic EML4-ALK by disruption of an atypical β-propeller domain."],"pmcid":["PMC3986153"],"funding_grant_id":["ST/J001511/1","12772","C24461/A13231"],"pubmed_authors":["Busacca S","Richards MW","Fennell DA","O'Regan L","Bayliss R","Law EW","Rennalls LP","Fry AM"],"additional_accession":[]},"is_claimable":false,"name":"Crystal structure of EML1 reveals the basis for Hsp90 dependence of oncogenic EML4-ALK by disruption of an atypical β-propeller domain.","description":"Proteins of the echinoderm microtubule-associated protein (EMAP)-like (EML) family contribute to formation of the mitotic spindle and interphase microtubule network. They contain a unique hydrophobic EML protein (HELP) motif and a variable number of WD40 repeats. Recurrent gene rearrangements in nonsmall cell lung cancer fuse EML4 to anaplastic lymphoma kinase (ALK), causing expression of several fusion oncoprotein variants. We have determined a 2.6-Å crystal structure of the representative ∼70-kDa core of EML1, revealing an intimately associated pair of β-propellers, which we term a TAPE (tandem atypical propeller in EMLs) domain. One propeller is highly atypical, having a discontinuous subdomain unrelated to a WD40 motif in place of one of its blades. This unexpected feature shows how a ","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Apr","modification":"2026-04-29T16:29:44.735Z","creation":"2019-03-27T01:24:57Z"},"accession":"S-EPMC3986153","cross_references":{"pubmed":["24706829"],"doi":["10.1073/pnas.1322892111"]}}