{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Suraweera CD"],"funding":["La Trobe University"],"pagination":["738"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9027176"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(4)"],"pubmed_abstract":["Numerous large DNA viruses have evolved sophisticated countermeasures to hijack the premature programmed cell death of host cells post-infection, including the expression of proteins homologous in sequence, structure, or function to cellular Bcl-2 proteins. Kaposi sarcoma herpes virus (KSHV), a member of the <i>gammaherpesvirinae</i>, has been shown to encode for KsBcl-2, a potent inhibitor of Bcl-2 mediated apoptosis. KsBcl-2 acts by directly engaging host pro-apoptotic Bcl-2 proteins including Bak, Bax and Bok, the BH3-only proteins; Bim, Bid, Bik, Hrk, Noxa and Puma. Here we determined the crystal structures of KsBcl-2 bound to the BH3 motif of pro-apoptotic proteins Bid and Puma. The structures reveal that KsBcl-2 engages pro-apoptotic BH3 motif peptides using the canonical ligand bind"],"journal":["Viruses"],"pubmed_title":["Structural Insight into KsBcl-2 Mediated Apoptosis Inhibition by Kaposi Sarcoma Associated Herpes Virus."],"pmcid":["PMC9027176"],"funding_grant_id":["n/a"],"pubmed_authors":["Suraweera CD","Hinds MG","Kvansakul M"],"additional_accession":[]},"is_claimable":false,"name":"Structural Insight into KsBcl-2 Mediated Apoptosis Inhibition by Kaposi Sarcoma Associated Herpes Virus.","description":"Numerous large DNA viruses have evolved sophisticated countermeasures to hijack the premature programmed cell death of host cells post-infection, including the expression of proteins homologous in sequence, structure, or function to cellular Bcl-2 proteins. Kaposi sarcoma herpes virus (KSHV), a member of the <i>gammaherpesvirinae</i>, has been shown to encode for KsBcl-2, a potent inhibitor of Bcl-2 mediated apoptosis. KsBcl-2 acts by directly engaging host pro-apoptotic Bcl-2 proteins including Bak, Bax and Bok, the BH3-only proteins; Bim, Bid, Bik, Hrk, Noxa and Puma. Here we determined the crystal structures of KsBcl-2 bound to the BH3 motif of pro-apoptotic proteins Bid and Puma. The structures reveal that KsBcl-2 engages pro-apoptotic BH3 motif peptides using the canonical ligand bind","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Mar","modification":"2025-04-20T03:06:32.865Z","creation":"2025-04-20T03:06:32.865Z"},"accession":"S-EPMC9027176","cross_references":{"pubmed":["35458468"],"doi":["10.3390/v14040738"]}}