7LGA
PEG10 CA-like C-terminal domain
Summary for 7LGA
| Entry DOI | 10.2210/pdb7lga/pdb |
| Descriptor | Retrotransposon-derived protein PEG10 (2 entities in total) |
| Functional Keywords | imprinted gene, domesticated gag, oncoprotein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 46807.75 |
| Authors | Zurowska, K.,Pornillos, O.,Ganser-Pornillos, B.K. (deposition date: 2021-01-19, release date: 2021-10-06, Last modification date: 2024-10-16) |
| Primary citation | Zurowska, K.,Alam, A.,Ganser-Pornillos, B.K.,Pornillos, O. Structural evidence that MOAP1 and PEG10 are derived from retrovirus/retrotransposon Gag proteins. Proteins, 90:309-313, 2022 Cited by 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 the key interactions that facilitated assembly of their ancestral Gags into capsids. PubMed: 34357660DOI: 10.1002/prot.26204 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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