Structural highlights
Function
[MOAP1_HUMAN] Required for death receptor-dependent apoptosis. When associated with RASSF1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF10 stimulation.[1]
Publication Abstract from PubMed
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.
Structural evidence that MOAP1 and PEG10 are derived from retrovirus/retrotransposon Gag proteins.,Zurowska K, Alam A, Ganser-Pornillos BK, Pornillos O Proteins. 2021 Aug 6. doi: 10.1002/prot.26204. PMID:34357660[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Baksh S, Tommasi S, Fenton S, Yu VC, Martins LM, Pfeifer GP, Latif F, Downward J, Neel BG. The tumor suppressor RASSF1A and MAP-1 link death receptor signaling to Bax conformational change and cell death. Mol Cell. 2005 Jun 10;18(6):637-50. PMID:15949439 doi:http://dx.doi.org/S1097-2765(05)01316-X
- ↑ Zurowska K, Alam A, Ganser-Pornillos BK, Pornillos O. Structural evidence that MOAP1 and PEG10 are derived from retrovirus/retrotransposon Gag proteins. Proteins. 2021 Aug 6. doi: 10.1002/prot.26204. PMID:34357660 doi:http://dx.doi.org/10.1002/prot.26204
