1y4m

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1y4m, resolution 1.60Å

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

Overview

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.

About this Structure

1Y4M is a Single protein structure of sequence from Homo sapiens with CL as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of a pivotal domain of human syncytin-2, a 40 million years old endogenous retrovirus fusogenic envelope gene captured by primates., Renard M, Varela PF, Letzelter C, Duquerroy S, Rey FA, Heidmann T, J Mol Biol. 2005 Oct 7;352(5):1029-34. PMID:16140326

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