{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hamza A"],"funding":["Council of Scientific and Industrial Research","Central Council for Research in Unani Medicine"],"pagination":["1950"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8880246"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(4)"],"pubmed_abstract":["Respiratory syncytial virus (RSV) is the leading cause of lower respiratory tract infection in children and infants. To date, there is no effective vaccine available against RSV. Heparan sulfate is a type of glycosaminoglycan that aids in the attachment of the RSV to the host cell membrane via the G protein. In the present study, the effect of amino acid substitution on the structure and stability of the ectodomain G protein was studied. Further, it was investigated whether mutation (K117A) in the CX3C motif of G protein alters the binding with heparan sulfate. The point mutation significantly affects the conformational stability of the G protein. The mutant protein showed a low binding affinity with heparan sulfate as compared to the wild-type G protein, as determined by fluorescence quen"],"journal":["International journal of molecular sciences"],"pubmed_title":["Mutation in the CX3C Motif of G Protein Disrupts Its Interaction with Heparan Sulfate: A Calorimetric, Spectroscopic, and Molecular Docking Study."],"pmcid":["PMC8880246"],"funding_grant_id":["RG-1439-74","37(1697)17/EMR-II","F.No.3-63/2019-CCRUM/Tech"],"pubmed_authors":["Hamza A","Almajhdi FN","Hussain T","Parveen S","Ara S","Ahmed A","Samad A","Islam A","Parray ZA"],"additional_accession":[]},"is_claimable":false,"name":"Mutation in the CX3C Motif of G Protein Disrupts Its Interaction with Heparan Sulfate: A Calorimetric, Spectroscopic, and Molecular Docking Study.","description":"Respiratory syncytial virus (RSV) is the leading cause of lower respiratory tract infection in children and infants. To date, there is no effective vaccine available against RSV. Heparan sulfate is a type of glycosaminoglycan that aids in the attachment of the RSV to the host cell membrane via the G protein. In the present study, the effect of amino acid substitution on the structure and stability of the ectodomain G protein was studied. Further, it was investigated whether mutation (K117A) in the CX3C motif of G protein alters the binding with heparan sulfate. The point mutation significantly affects the conformational stability of the G protein. The mutant protein showed a low binding affinity with heparan sulfate as compared to the wild-type G protein, as determined by fluorescence quen","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Feb","modification":"2025-04-19T10:50:55.362Z","creation":"2024-11-15T00:29:13.257Z"},"accession":"S-EPMC8880246","cross_references":{"pubmed":["35216066"],"doi":["10.3390/ijms23041950"]}}