1y4m

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(New page: 200px<br /> <applet load="1y4m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y4m, resolution 1.60&Aring;" /> '''Crystal structure o...)
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[[Image:1y4m.gif|left|200px]]<br />
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[[Image:1y4m.gif|left|200px]]<br /><applet load="1y4m" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1y4m" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1y4m, resolution 1.60&Aring;" />
caption="1y4m, resolution 1.60&Aring;" />
'''Crystal structure of human endogenous retrovirus HERV-FRD envelope protein (syncitin-2)'''<br />
'''Crystal structure of human endogenous retrovirus HERV-FRD envelope protein (syncitin-2)'''<br />
==Overview==
==Overview==
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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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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==
==About this Structure==
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1Y4M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y4M OCA].
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1Y4M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y4M OCA].
==Reference==
==Reference==
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[[Category: Letzelter, C.]]
[[Category: Letzelter, C.]]
[[Category: Renard, M.]]
[[Category: Renard, M.]]
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[[Category: Rey, F.A.]]
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[[Category: Rey, F A.]]
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[[Category: Varela, P.F.]]
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[[Category: Varela, P F.]]
[[Category: CL]]
[[Category: CL]]
[[Category: coat protein]]
[[Category: coat protein]]
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[[Category: membrane fusion]]
[[Category: membrane fusion]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:14:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:44 2008''

Revision as of 14:01, 21 February 2008


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 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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