{"doi":"10.1074/jbc.m111.337741","title":"Distinct Properties of Glycine Receptor β+/α− Interface","abstract":null,"journal":"Journal of Biological Chemistry","year":2012,"id":661665,"datarank":0.31191623125197543,"base_score":2.0794415416798357,"endowment":2.0794415416798357,"self_citation_contribution":0.31191623125197543,"citation_network_contribution":0.0,"self_endowment_contribution":0.31191623125197543,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":7,"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":1477192,"name":"Lu Han","orcid":"0000-0001-6520-6083","position":1,"is_corresponding":false},{"id":481316,"name":"Joseph W. Lynch","orcid":"0000-0002-1227-2252","position":2,"is_corresponding":false},{"id":286407,"name":"Qiang Shan","orcid":"0000-0002-7089-0278","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Distinct Properties of Glycine Receptor β+/α− Interface","abstract":"The glycine receptor (GlyR) exists either in homomeric α or heteromeric αβ forms. Its agonists bind at extracellular subunit interfaces. Unlike subunit interfaces from the homomeric α GlyR, subunit interfaces from the heteromeric αβ GlyR have not been characterized unambiguously because of the existence of multiple types of interface within single receptors. Here, we report that, by reconstituting β+/α- interfaces in a homomeric GlyR (αChb+a- GlyR), we were able to functionally characterize the αβ GlyR β+/α- interfaces. We found that the β+/α- interface had a higher agonist sensitivity than that of the α+/α- interface. This high sensitivity was contributed primarily by loop A. We also found that the β+/α- interface differentially modulates the agonist properties of glycine and taurine. Using voltage clamp fluorometry, we found that the conformational changes induced by glycine binding to the β+/α- interface were different from those induced by glycine binding to the α+/α- interface in the α GlyR. Moreover, the distinct conformational changes found at the β+/α- interface in the αChb+a- GlyR were also found in the heteromeric αβ GlyR, which suggests that the αChb+a- GlyR reconstitutes structural components and recapitulates functional properties, of the β+/α- interface in the heteromeric αβ GlyR. Our investigation not only provides structural and functional information about the GlyR β+/α- interface, which could direct GlyR β+/α- interface-specific drug design, but also provides a general methodology for unambiguously characterizing properties of specific protein interfaces from heteromeric proteins.","is_dataset_classified":null,"base_score":2.0794415416798357,"endowment":2.0794415416798357,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"22535951","pmcid":"PMC3375546","openalex_id":"https://openalex.org/W2120205640","authors":[],"funders":[],"total_grants":0,"fwci":0.1228,"citation_percentile":0.50015358,"influential_citations":0,"citation_trend":[{"year":2014,"count":1},{"year":2016,"count":2},{"year":2019,"count":1},{"year":2020,"count":1},{"year":2021,"count":1},{"year":2025,"count":1}],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"http://www.jbc.org/article/S0021925820498163/pdf","host_type":"journal"},{"url":"http://www.jbc.org/article/S0021925820498163/pdf","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925820498163?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925820498163?httpAccept=text/plain","host_type":"publisher"},{"url":"https://syndication.highwire.org/content/doi/10.1074/jbc.M111.337741","host_type":"publisher"},{"url":"https://doi.org/10.1074/jbc.m111.337741","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/22535951","host_type":"repository"},{"url":"http://europepmc.org/articles/PMC3375546","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3375546","host_type":"repository"}],"fields_of_study":["Nicotinic Acetylcholine Receptors Study","Receptor Mechanisms and Signaling","Neuroscience and Neuropharmacology Research","Animals","Glycine","HEK293 Cells","Humans","Protein Multimerization","Protein Structure, Quaternary","Receptors, Glycine","Structure-Activity Relationship","Xenopus laevis"],"mesh_terms":["Animals","Glycine","Humans","Structure-Activity Relationship","Xenopus laevis","Receptors, Glycine","Protein Structure, Quaternary","Protein Multimerization","HEK293 Cells"],"keywords":["Homomeric","Glycine receptor","Glycine","Chemistry","Protein subunit","Biophysics","Biochemistry","Biology","Amino acid"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-12T11:25:08.452846Z","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":[]}