Crystal structure of a pivotal domain of human syncytin-2, a 40 million years old endogenous retrovirus fusogenic envelope gene captured by primates.
J Mol Biol
; 352(5): 1029-34, 2005 Oct 07.
Article
in En
| MEDLINE
| ID: mdl-16140326
ABSTRACT
HERV-FRD is a human endogenous retrovirus that entered the human genome 40 million years ago. Its envelope gene, syncytin-2, was diverted by an ancestral host most probably because of its fusogenic property, for a role in placenta morphogenesis. It was maintained in a functional state in all primate branches as a bona fide cellular gene, submitted to a very low mutation rate as compared to infectious retrovirus genomes. The structure of the syncytin-2 protein thus provides a good insight into that of the oldest mammalian retroviral envelope. Here, we report the crystal structure of a central fragment of its "fossil" ectodomain, allowing a remarkable superposition with the structures of the corresponding domains of present-day infectious retroviruses, in spite of a more than 60% divergent sequence. These results suggest the existence of a unique structural solution selected by these proteins for their fusogenic function.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Pregnancy Proteins
/
Primates
/
Retroviridae
/
Viral Proteins
/
Gene Products, env
Limits:
Animals
/
Humans
Language:
En
Journal:
J Mol Biol
Year:
2005
Document type:
Article
Affiliation country:
France