2rm4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2rm4.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2rm4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2rm4| PDB=2rm4 | SCENE= }}
{{STRUCTURE_2rm4| PDB=2rm4 | SCENE= }}
-
'''Solution Structure of the LSM Domain of Dm EDC3 (Enhancer of DECAPPING 3)'''
+
===Solution Structure of the LSM Domain of Dm EDC3 (Enhancer of DECAPPING 3)===
-
==Overview==
+
<!--
-
Members of the (L)Sm (Sm and Sm-like) 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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17923697}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17923697 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17923697}}
==About this Structure==
==About this Structure==
-
2RM4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RM4 OCA].
+
2RM4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RM4 OCA].
==Reference==
==Reference==
Line 29: Line 33:
[[Category: Protein binding]]
[[Category: Protein binding]]
[[Category: Sm-like protein]]
[[Category: Sm-like protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:09:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:52:49 2008''

Revision as of 10:52, 28 July 2008

Image:2rm4.png

Template:STRUCTURE 2rm4

Solution Structure of the LSM Domain of Dm EDC3 (Enhancer of DECAPPING 3)

Template:ABSTRACT PUBMED 17923697

About this Structure

2RM4 is a Single protein structure of sequence from Drosophila melanogaster. Full experimental 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 Dec;27(24):8600-11. Epub 2007 Oct 8. PMID:17923697

Page seeded by OCA on Mon Jul 28 13:52:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rm4"
Personal tools