{"doi":"10.1073/pnas.95.14.7909","title":"Solution structure of the cytohesin-1 (B2–1) Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1","abstract":"<jats:p>\n                    Cytohesin-1 (B2–1) is a guanine nucleotide exchange factor for human ADP ribosylation factor (Arf) GTPases, which are important for vesicular protein trafficking and coatamer assembly in the cell. Cytohesin-1 also has been reported to promote cellular adhesion via binding to the β2 integrin cytoplasmic domain. The solution structure of the Sec7 domain of cytohesin-1, which is responsible for both the protein’s guanine nucleotide exchange factor function and β2 integrin binding, was determined by NMR spectroscopy. The structure consists of 10 α-helices that form a unique tertiary fold. The binding between the Sec7 domain and a soluble, truncated version of human Arf-1 was investigated by examining\n                    <jats:sup>1</jats:sup>\n                    H-\n                    <jats:sup>15</jats:sup>\n                    N and\n                    <jats:sup>1</jats:sup>\n                    H-\n                    <jats:sup>13</jats:sup>\n                    C chemical shift changes between the native protein and the Sec7/Arf-1 complex. We show that the binding to Arf-1 occurs through a large surface on the C-terminal subdomain that is composed of both hydrophobic and polar residues. Structure-based mutational analysis of the cytohesin-1 Sec7 domain has been used to identify residues important for binding to Arf and for mediating nucleotide exchange. Investigations into the interaction between the Sec7 domain and the β2 integrin cytoplasmic domain suggest that the two proteins do not interact in the solution phase.\n                  </jats:p>","journal":"Proceedings of the National Academy of Sciences","year":1998,"id":662178,"datarank":0.5456379239589579,"base_score":3.6375861597263857,"endowment":3.6375861597263857,"self_citation_contribution":0.5456379239589579,"citation_network_contribution":0.0,"self_endowment_contribution":0.5456379239589579,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":37,"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":1728656,"name":"Arndt Schnuchel","orcid":null,"position":1,"is_corresponding":false},{"id":598781,"name":"Hong Wang","orcid":"0000-0002-0213-3523","position":2,"is_corresponding":false},{"id":498408,"name":"Edward T. Olejniczak","orcid":null,"position":3,"is_corresponding":false},{"id":1728657,"name":"Robert P. Meadows","orcid":null,"position":4,"is_corresponding":false},{"id":1728658,"name":"Brian P. Lipsky","orcid":null,"position":5,"is_corresponding":false},{"id":1728659,"name":"Edith A. S. Harris","orcid":null,"position":6,"is_corresponding":false},{"id":1728660,"name":"Donald E. Staunton","orcid":null,"position":7,"is_corresponding":false},{"id":289615,"name":"Stephen W. Fesik","orcid":"0000-0001-5957-6192","position":8,"is_corresponding":false},{"id":529122,"name":"Stephen F. Betz","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Solution structure of the cytohesin-1 (B2–1) Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1","abstract":"<jats:p>\n                    Cytohesin-1 (B2–1) is a guanine nucleotide exchange factor for human ADP ribosylation factor (Arf) GTPases, which are important for vesicular protein trafficking and coatamer assembly in the cell. Cytohesin-1 also has been reported to promote cellular adhesion via binding to the β2 integrin cytoplasmic domain. The solution structure of the Sec7 domain of cytohesin-1, which is responsible for both the protein’s guanine nucleotide exchange factor function and β2 integrin binding, was determined by NMR spectroscopy. The structure consists of 10 α-helices that form a unique tertiary fold. The binding between the Sec7 domain and a soluble, truncated version of human Arf-1 was investigated by examining\n                    <jats:sup>1</jats:sup>\n                    H-\n                    <jats:sup>15</jats:sup>\n                    N and\n                    <jats:sup>1</jats:sup>\n                    H-\n                    <jats:sup>13</jats:sup>\n                    C chemical shift changes between the native protein and the Sec7/Arf-1 complex. We show that the binding to Arf-1 occurs through a large surface on the C-terminal subdomain that is composed of both hydrophobic and polar residues. Structure-based mutational analysis of the cytohesin-1 Sec7 domain has been used to identify residues important for binding to Arf and for mediating nucleotide exchange. Investigations into the interaction between the Sec7 domain and the β2 integrin cytoplasmic domain suggest that the two proteins do not interact in the solution phase.\n                  </jats:p>","is_dataset_classified":null,"base_score":3.6375861597263857,"endowment":3.6375861597263857,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"9653114","pmcid":"PMC20903","openalex_id":"https://openalex.org/W2016052537","authors":[],"funders":[{"funder_name":"NCRR NIH HHS","grant_id":"P41 RR002301","title":null},{"funder_name":"NCRR NIH HHS","grant_id":"S10 RR002781","title":null},{"funder_name":"NCRR NIH HHS","grant_id":"S10 RR008438","title":null},{"funder_name":"NCRR NIH HHS","grant_id":"RR02301","title":null}],"total_grants":4,"fwci":2.1316,"citation_percentile":0.8738305,"influential_citations":0,"citation_trend":[{"year":2014,"count":1},{"year":2015,"count":1},{"year":2017,"count":1},{"year":2019,"count":1}],"oa_status":"green","license":null,"oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/20903","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/20903","host_type":"repository"},{"url":"https://pnas.org/doi/pdf/10.1073/pnas.95.14.7909","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.95.14.7909","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/9653114","host_type":"repository"}],"fields_of_study":["Cellular transport and secretion","Microtubule and mitosis dynamics","Lipid Membrane Structure and Behavior"],"mesh_terms":["Amino Acid Sequence","Binding Sites","Biological Transport","Cloning, Molecular","Humans","Molecular Sequence Data","Protein Binding","Cell Adhesion Molecules","Protein Structure, Secondary","Protein Folding","CD18 Antigens","GTP-Binding Proteins","Guanine Nucleotide Exchange Factors","ADP-Ribosylation Factors"],"keywords":["ADP ribosylation factor","Guanine nucleotide exchange factor","Chemistry","Cyclic nucleotide-binding domain","GTPase","EGF-like domain","Plasma protein binding","ADP-ribosylation","Cytoplasm","GTPase-activating protein","Cell biology","Biochemistry","Binding domain","Nucleotide","Binding site","Biology","G protein","Receptor","Cell","NAD+ kinase","Golgi apparatus","Gene"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-12T13:02:49.839980Z","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":[]}