Related Experiment Video
Updated: Oct 25, 2025

Visualization of HIV-1 Gag Binding to Giant Unilamellar Vesicle GUV Membranes
Published on: July 28, 2016
Structural evidence that MOAP1 and PEG10 are derived from retrovirus/retrotransposon Gag proteins
Katarzyna Zurowska1, Ayaan Alam1, Barbie K Ganser-Pornillos1
1Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA.
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.
More Related Videos
Related Concept Videos
Retroviruses
LTR Retrotransposons
The internal coding region of LTR retrotransposons and their mechanism of transposition closely resembles a...
Retrovirus Life Cycles
Non-LTR Retrotransposons
DNA-only Transposons
The donor site from where the transposon is excised is either degraded or...
Mechanisms of Retrovirus-induced Cancers

