2vc8
From Proteopedia
(New page: 200px<br /> <applet load="2vc8" size="450" color="white" frame="true" align="right" spinBox="true" caption="2vc8, resolution 1.31Å" /> '''CRYSTAL STRUCTURE O...) |
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| - | [[Image:2vc8.gif|left|200px]]<br /> | + | [[Image:2vc8.gif|left|200px]]<br /><applet load="2vc8" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="2vc8, resolution 1.31Å" /> | caption="2vc8, resolution 1.31Å" /> | ||
'''CRYSTAL STRUCTURE OF THE LSM DOMAIN OF HUMAN EDC3 (ENHANCER OF DECAPPING 3)'''<br /> | '''CRYSTAL STRUCTURE OF THE LSM DOMAIN OF HUMAN EDC3 (ENHANCER OF DECAPPING 3)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2VC8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2VC8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VC8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: sm-like protein]] | [[Category: sm-like protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:41:04 2008'' |
Revision as of 09:41, 23 January 2008
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CRYSTAL STRUCTURE OF THE LSM DOMAIN OF HUMAN EDC3 (ENHANCER OF DECAPPING 3)
Overview
Members of the (L)Sm (Sm and Like-Sm) protein family are found across all, kingdoms of life and play crucial roles in RNA metabolism. The P-body, component EDC3 (enhancer of decapping 3) is a divergent member of this, family that functions in mRNA decapping. EDC3 is composed of a N-terminal, LSm domain, a central FDF domain and a C-terminal YjeF-N domain. We show, that this modular architecture enables EDC3 to interact with multiple, components of the decapping machinery, including DCP1, DCP2 and Me31B. The, LSm domain mediates DCP1-binding and P-body localization. We determined, the three-dimensional structures of the LSm domains of Drosophila, melanogaster and human EDC3 and show that the domain adopts a divergent, Sm-fold that lacks the characteristic N-terminal alpha-helix and has a, disrupted beta4-strand. This domain remains monomeric in solution and, lacks several features that canonical (L)Sm domains require for binding, RNA. The structures also revealed a conserved patch of surface residues, that are required for the interaction with DCP1, but not for P-body, localization. The conservation of surface and of critical structural, residues indicates that LSm domains in EDC3 proteins adopt a similar fold, that has separable novel functions that are absent in canonical (L)Sm, proteins.
About this Structure
2VC8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
A divergent Sm-fold in EDC3 proteins mediates DCP1-binding and P-body targeting., Tritschler F, Eulalio A, Truffault V, Hartmann MD, Helms S, Schmidt S, Coles M, Izaurralde E, Weichenrieder O, Mol Cell Biol. 2007 Oct 8;. PMID:17923697
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