{"doi":"10.1016/j.sciaf.2020.e00510","title":"Brownian dynamics simulations of the interactions between lactate dehydrogenase (LDH) and G- or F-Actin. Part I: Muscle and heart homo-isoforms","abstract":"Glycolytic enzymes may compartment in cells by binding to cytoskeletal structures. One potentially important step in compartmentation is the binding of the cytoskeletal protein F-actin by lactate dehydrogenase (LDH). Brownian dynamics (BD) simulations of LDH interacting with G- or F-actin provided first-encounter snapshots and relative binding free energies. Models of muscle (LDH-M4) and heart (LDH-H4) isoforms of lactate dehydrogenase for four species (rabbit, human, rat and pig) were examined. Strong electrostatic interactions were observed between both monomeric and polymerized actin for LDH-M4, but not LDH-H4. These electrostatic field potentials were examined in detail and explained the differences in complex formations between LDH-M4 and LDH-H4 with G- and F-actin. Complexes formed between LDH-M4 and G-actin involved residues found in the surface grooves between the A/D and B/C subunits. Several binding modes occurred between LDH-M4 and F-actin, the most frequent of which involved two subunits of actin interacting with two subunits of LDH-M4. LDH-M4 interactions with F-actin relied on 10 residues, nine of which were conserved between species. All of these residues except two were located in the positive grooves between A/D and B/C subunits, where the protein's electrostatic potential is enhanced by its quaternary structure. LDH-H4, however, does not show unique binding modes nor does it have a favorable relative binding free energy compared to LDH-M4. Thus, BD supports experimental findings [Ehmann, J. D.; Hultin, H. O. Arch. Biochem. Biophys. 1973, 154, 471], that LDH-M4 binds actin, but LDH-H4 does not.","journal":"Scientific African","year":2020,"id":85682,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":3,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":0.9368,"is_data_producer":false,"deposit_databanks":null,"is_oa":true,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":"2020-01-01","fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":437876,"name":"Issofa Patouossa","orcid":"0000-0001-6761-9295","position":1,"is_corresponding":false},{"id":438722,"name":"Kristine L. Carlson","orcid":null,"position":2,"is_corresponding":false},{"id":438723,"name":"Stephen L. Lowe","orcid":null,"position":3,"is_corresponding":false},{"id":437877,"name":"Neville Y. Forlemu","orcid":"0000-0003-4083-8804","position":4,"is_corresponding":false},{"id":438724,"name":"Kathryn A. Thomasson","orcid":null,"position":5,"is_corresponding":false},{"id":437875,"name":"Eric N. Njabon","orcid":"0000-0003-2159-3418","position":0,"is_corresponding":true}],"reference_count":35,"raw_metadata":null,"created_at":"2026-07-18T21:58:16.217017Z","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":[]}