{"doi":"10.1016/j.str.2016.07.014","title":"Tankyrase-1 Ankyrin Repeats Form an Adaptable Binding Platform for Targets of ADP-Ribose Modification","abstract":null,"journal":"Structure","year":2016,"id":616924,"datarank":2.0525852855485693,"base_score":4.127134385045092,"endowment":4.127134385045092,"self_citation_contribution":0.6190701577567639,"citation_network_contribution":1.4335151277918057,"self_endowment_contribution":0.6190701577567639,"citer_contribution":1.4335151277918057,"corpus_percentile":null,"corpus_rank":null,"citation_count":61,"citer_count":55,"citers_with_citation_signal":48,"citers_with_endowment":48,"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":1590742,"name":"Michael McCauley","orcid":null,"position":1,"is_corresponding":false},{"id":232702,"name":"Marie-France Langelier","orcid":"0000-0001-9815-1840","position":2,"is_corresponding":false},{"id":361197,"name":"Kushol Gupta","orcid":"0000-0002-7006-2667","position":3,"is_corresponding":false},{"id":1590744,"name":"Swati Roy","orcid":null,"position":4,"is_corresponding":false},{"id":1590746,"name":"Gregory D. Van Duyne","orcid":null,"position":5,"is_corresponding":false},{"id":1590747,"name":"John M. Pascal","orcid":null,"position":6,"is_corresponding":false},{"id":376058,"name":"Travis Eisemann","orcid":"0000-0003-3602-2677","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Tankyrase-1 Ankyrin Repeats Form an Adaptable Binding Platform for Targets of ADP-Ribose Modification","abstract":"The poly(ADP-ribose) polymerase enzyme Tankyrase-1 (TNKS) regulates multiple cellular processes and interacts with diverse proteins using five ankyrin repeat clusters (ARCs). There are limited structural insights into functional roles of the multiple ARCs of TNKS. Here we present the ARC1-3 crystal structure and employ small-angle X-ray scattering (SAXS) to investigate solution conformations of the complete ankyrin repeat domain. Mutagenesis and binding studies using the bivalent TNKS binding domain of Axin1 demonstrate that only certain ARC combinations function together. The physical basis for these restrictions is explained by both rigid and flexible ankyrin repeat elements determined in our structural analysis. SAXS analysis is consistent with a dynamic ensemble of TNKS ankyrin repeat conformations modulated by Axin1 interaction. TNKS ankyrin repeat domain is thus an adaptable binding platform with structural features that can explain selectivity toward diverse proteins, and has implications for TNKS positioning of bound targets for poly(ADP-ribose) modification.","is_dataset_classified":null,"base_score":4.127134385045092,"endowment":4.127134385045092,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"27594684","pmcid":null,"openalex_id":"https://openalex.org/W2518534345","authors":[],"funders":[{"funder_name":"NIH","grant_id":"GM087282","title":null},{"funder_name":"NIH","grant_id":"GM100836","title":null},{"funder_name":"NCI","grant_id":"P30 CA56036","title":null},{"funder_name":"NIGMS","grant_id":"OD017987","title":null},{"funder_name":"NIGMS","grant_id":"GM103485","title":null},{"funder_name":"NSF","grant_id":"DMR-1332208","title":null},{"funder_name":"NSF","grant_id":"CHE-1265821","title":null},{"funder_name":"EPSRC","grant_id":"EP/K039121/1","title":"SI2-CHE: CCP-SAS - Collaborative Computational Project for advanced analyses of structural data in chemical biology and soft condensed matter"},{"funder_name":"National Institutes of Health","grant_id":"4P41GM103485-34","title":"Macromolecular Diffraction Resource: MacCHESS"},{"funder_name":"National Institutes of Health","grant_id":"5R01GM087282-04","title":"Structural Biochemistry of PARP-1"},{"funder_name":"National Science Foundation","grant_id":"1332208","title":"OPERATION OF CORNELL HIGH ENERGY SYNCHROTRON SOURCE (CHESS)"},{"funder_name":"National Institutes of Health","grant_id":"1S10OD017987-01","title":"A NEW HYBRID DIFFRACTOMETER FOR MACROMOLECULAR CRYSTALLOGRAPHY AND SAXS AT TJU"},{"funder_name":"National Science Foundation","grant_id":"1265821","title":"SI2-CHE: CCP-SAS - Collaborative Computing consortium for advanced analyses of structural data in chemical biology and soft condensed matter"},{"funder_name":"National Institutes of Health","grant_id":"3P30CA056036-22S1","title":"Strengthening Community Engagement in Colorectal Cancer Screening and Clinical Trial Enrollment Through a Community Health Educator"},{"funder_name":"National Institutes of Health","grant_id":"5T32GM100836-02","title":"Training Program in Cellular, Biochemical, and Molecular Sciences"}],"total_grants":15,"fwci":4.1145,"citation_percentile":0.94242814,"influential_citations":0,"citation_trend":[{"year":2016,"count":1},{"year":2017,"count":5},{"year":2018,"count":4},{"year":2019,"count":12},{"year":2020,"count":7},{"year":2021,"count":7},{"year":2022,"count":7},{"year":2023,"count":8},{"year":2024,"count":3},{"year":2025,"count":5},{"year":2026,"count":2}],"oa_status":"bronze","license":"Elsevier Non-Commercial","oa_locations":[{"url":"http://www.cell.com/article/S0969212616302258/pdf","host_type":"journal"},{"url":"http://www.cell.com/article/S0969212616302258/pdf","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0969212616302258?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0969212616302258?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.str.2016.07.014","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/27594684","host_type":"repository"},{"url":"https://dx.doi.org/10.1016/j.str.2016.07.014","host_type":""}],"fields_of_study":["Erythrocyte Function and Pathophysiology","Wnt/β-catenin signaling in development and cancer","Pancreatic function and diabetes","0301 basic medicine","0303 health sciences","03 medical and health sciences","Adenosine Diphosphate Ribose","Ankyrin Repeat","Axin Protein","Crystallography, X-Ray","Humans","Models, Molecular","Mutagenesis","Protein Binding","Protein Conformation","Protein Structure, Secondary","Scattering, Small Angle","Substrate Specificity","Tankyrases"],"mesh_terms":["Adenosine Diphosphate Ribose","Humans","Models, Molecular","Protein Binding","Protein Conformation","Substrate Specificity","Mutagenesis","Ankyrin Repeat","Protein Structure, Secondary","Crystallography, X-Ray","Tankyrases","Scattering, Small Angle","Axin Protein"],"keywords":["Ankyrin repeat","Ankyrin","Poly ADP ribose polymerase","Chemistry","Computational biology","Biochemistry","Cell biology","Genetics","Biology","DNA","Gene","Polymerase","Models, Molecular","Adenosine Diphosphate Ribose","Tankyrases","Protein Conformation","Crystallography, X-Ray","Protein Structure, Secondary","Substrate Specificity","Axin Protein","Mutagenesis","Scattering, Small Angle","Humans","Protein Binding"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-03T00:21:57.743615Z","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":[]}