1Y4M
Crystal structure of human endogenous retrovirus HERV-FRD envelope protein (syncitin-2)
Summary for 1Y4M
| Entry DOI | 10.2210/pdb1y4m/pdb |
| Related | 1MG1 1MOF |
| Descriptor | HERV-FRD_6p24.1 provirus ancestral Env polyprotein, CHLORIDE ION (3 entities in total) |
| Functional Keywords | coat protein, membrane fusion, endogenous retrovirus, membrane protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Virion. Transmembrane protein: Cell membrane; Single-pass membrane protein (Potential): P60508 |
| Total number of polymer chains | 3 |
| Total formula weight | 17404.64 |
| 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 citation | Renard, 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: 16140326DOI: 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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