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1Y4M

Crystal structure of human endogenous retrovirus HERV-FRD envelope protein (syncitin-2)

Summary for 1Y4M
Entry DOI10.2210/pdb1y4m/pdb
Related1MG1 1MOF
DescriptorHERV-FRD_6p24.1 provirus ancestral Env polyprotein, CHLORIDE ION (3 entities in total)
Functional Keywordscoat protein, membrane fusion, endogenous retrovirus, membrane protein
Biological sourceHomo sapiens (human)
Cellular locationVirion. Transmembrane protein: Cell membrane; Single-pass membrane protein (Potential): P60508
Total number of polymer chains3
Total formula weight17404.64
Authors
Renard, M.,Varela, P.F.,Letzelter, C.,Duquerroy, S.,Rey, F.A.,Heidmann, T. (deposition date: 2004-12-01, release date: 2005-11-15, Last modification date: 2024-11-06)
Primary citationRenard, M.,Varela, P.F.,Letzelter, C.,Duquerroy, S.,Rey, F.A.,Heidmann, T.
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., 352:1029-1034, 2005
Cited by
PubMed 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.
PubMed: 16140326
DOI: 10.1016/j.jmb.2005.07.058
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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