{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zurowska K"],"funding":["National Institute of Allergy and Infectious Diseases","NIAID NIH HHS"],"pagination":["309-313"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8671222"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["90(1)"],"pubmed_abstract":["The Gag proteins of retroviruses play an essential role in virus particle assembly by forming a protein shell or capsid and thus generating the virion compartment. A variety of human proteins have now been identified with structural similarity to one or more of the major Gag domains. These human proteins are thought to have been evolved or \"domesticated\" from ancient integrations due to retroviral infections or retrotransposons. Here, we report that X-ray crystal structures of stably folded domains of MOAP1 (modulator of apoptosis 1) and PEG10 (paternally expressed gene 10) are highly similar to the C-terminal capsid (CA) domains of cognate Gag proteins. The structures confirm classification of MOAP1 and PEG10 as domesticated Gags, and suggest that these proteins may have preserved some of"],"journal":["Proteins"],"pubmed_title":["Structural evidence that MOAP1 and PEG10 are derived from retrovirus/retrotransposon Gag proteins."],"pmcid":["PMC8671222"],"funding_grant_id":["R01 AI129678","R01‐AI129678"],"pubmed_authors":["Alam A","Ganser-Pornillos BK","Pornillos O","Zurowska K"],"additional_accession":[]},"is_claimable":false,"name":"Structural evidence that MOAP1 and PEG10 are derived from retrovirus/retrotransposon Gag proteins.","description":"The Gag proteins of retroviruses play an essential role in virus particle assembly by forming a protein shell or capsid and thus generating the virion compartment. A variety of human proteins have now been identified with structural similarity to one or more of the major Gag domains. These human proteins are thought to have been evolved or \"domesticated\" from ancient integrations due to retroviral infections or retrotransposons. Here, we report that X-ray crystal structures of stably folded domains of MOAP1 (modulator of apoptosis 1) and PEG10 (paternally expressed gene 10) are highly similar to the C-terminal capsid (CA) domains of cognate Gag proteins. The structures confirm classification of MOAP1 and PEG10 as domesticated Gags, and suggest that these proteins may have preserved some of","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jan","modification":"2025-04-22T10:08:13.958Z","creation":"2025-04-05T23:29:35.587Z"},"accession":"S-EPMC8671222","cross_references":{"pubmed":["34357660"],"doi":["10.1002/prot.26204"]}}