{"doi":"10.1074/jbc.m109.083048","title":"A Fused α-β “Mini-spectrin” Mimics the Intact Erythrocyte Spectrin Head-to-head Tetramer","abstract":null,"journal":"Journal of Biological Chemistry","year":2010,"id":654830,"datarank":0.4566783656585135,"base_score":3.044522437723423,"endowment":3.044522437723423,"self_citation_contribution":0.4566783656585135,"citation_network_contribution":0.0,"self_endowment_contribution":0.4566783656585135,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":20,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":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":1709065,"name":"Donghai Li","orcid":null,"position":1,"is_corresponding":false},{"id":1709066,"name":"Yelena Maksimova","orcid":null,"position":2,"is_corresponding":false},{"id":191293,"name":"Patrick G. Gallagher","orcid":null,"position":3,"is_corresponding":false},{"id":258005,"name":"David W. Speicher","orcid":"0000-0003-1311-4261","position":4,"is_corresponding":false},{"id":874938,"name":"Sandra L. Harper","orcid":"0000-0002-3036-6893","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"A fused alpha-beta \"mini-spectrin\" mimics the intact erythrocyte spectrin head-to-head tetramer.","abstract":"Head-to-head assembly of two spectrin heterodimers to form an actin-cross-linking tetramer is a physiologically dynamic interaction that contributes to red cell membrane integrity. Recombinant beta-spectrin C-terminal and alpha-spectrin N-terminal peptides can form tetramer-like univalent complexes, but they cannot evaluate effects of the open-closed dimer interactions or lateral associations of the two-spectrin strands on tetramer formation. In this study we produced and characterized a fused \"mini-spectrin dimer\" containing the beta-spectrin C-terminal region linked to the alpha-spectrin N-terminal region. This fused mini-spectrin mimics structural and functional properties of intact, full-length dimers and tetramers, including lateral association of the alpha and beta subunits in the dimer and formation of a closed dimer. High performance liquid chromatography gel filtration analyses of this mini-spectrin provide the first direct non-imaging experimental evidence for open and closed spectrin dimers and show that dimer-tetramer-oligomer interconversion is slow at low temperatures and accelerated at 30 degrees C, analogous to full-length spectrin. This protein exhibits wild type dimer-tetramer dissociation constants of approximately 1 mum at 30 degrees C, independent of initial oligomeric state. Conformational states of the mini-spectrin dimer were probed further using chemical cross-linking, which identified distinct groups of cross-links for \"open\" and \"closed\" dimers and confirmed the N-terminal region of alpha-spectrin remains highly flexible in the complex, exhibiting closely analogous structures to those observed for the isolated alpha-spectrin N-terminal using NMR (Park, S., Caffrey, M. S., Johnson, M. E., and Fung, L. W. (2003) J. Biol. Chem. 278, 21837-21844). This fusion protein should serve as a useful template for structural and functional studies of the divalent tetramer site.","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"20139081","pmcid":"PMC2856305","openalex_id":null,"authors":[],"funders":[{"funder_name":"NHLBI NIH HHS","grant_id":"HL65448","title":null},{"funder_name":"NCI NIH HHS","grant_id":"P30 CA010815","title":null},{"funder_name":"NHLBI NIH HHS","grant_id":"R01 HL065448","title":null},{"funder_name":"NHLBI NIH HHS","grant_id":"HL38794","title":null},{"funder_name":"NHLBI NIH HHS","grant_id":"R01 HL038794","title":null}],"total_grants":5,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"http://www.jbc.org/article/S0021925820747587/pdf","host_type":"publisher"},{"url":"http://www.jbc.org/content/285/14/11003.full.pdf","host_type":"Unpaywall"}],"fields_of_study":[],"mesh_terms":["Erythrocytes","Humans","Spectrin","Cross-Linking Reagents","Chromatography, Gel","Chromatography, High Pressure Liquid","Biomimetics","Protein Conformation","Dimerization","Protein Multimerization"],"keywords":[],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-11T08:34:57.704904Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}