This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2kxq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2kxq.png|left|200px]]
 
- 
{{STRUCTURE_2kxq| PDB=2kxq | SCENE= }}
{{STRUCTURE_2kxq| PDB=2kxq | SCENE= }}
- 
===Solution Structure of Smurf2 WW2 and WW3 bound to Smad7 PY motif containing peptide===
===Solution Structure of Smurf2 WW2 and WW3 bound to Smad7 PY motif containing peptide===
 +
{{ABSTRACT_PUBMED_20937913}}
-
{{ABSTRACT_PUBMED_20937913}}
+
==Function==
 +
[[http://www.uniprot.org/uniprot/SMUF2_HUMAN SMUF2_HUMAN]] E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD1 and SMAD7 in order to trigger their ubiquitination and proteasome-dependent degradation. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with SCYE1. Forms a stable complex with the TGF-beta receptor-mediated phosphorylated SMAD2 and SMAD3. In this way, SMAD2 may recruit substrates, such as SNON, for ubiquitin-mediated degradation. Enhances the inhibitory activity of SMAD7 and reduces the transcriptional activity of SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable decrease in steady-state level of SMAD1 protein and a smaller decrease of SMAD2 level.<ref>PMID:11389444</ref><ref>PMID:12717440</ref>
==About this Structure==
==About this Structure==
Line 11: Line 10:
==Reference==
==Reference==
-
<ref group="xtra">PMID:020937913</ref><references group="xtra"/>
+
<ref group="xtra">PMID:020937913</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Chong, A.]]
[[Category: Chong, A.]]

Revision as of 20:03, 24 March 2013

Template:STRUCTURE 2kxq

Contents

Solution Structure of Smurf2 WW2 and WW3 bound to Smad7 PY motif containing peptide

Template:ABSTRACT PUBMED 20937913

Function

[SMUF2_HUMAN] E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD1 and SMAD7 in order to trigger their ubiquitination and proteasome-dependent degradation. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with SCYE1. Forms a stable complex with the TGF-beta receptor-mediated phosphorylated SMAD2 and SMAD3. In this way, SMAD2 may recruit substrates, such as SNON, for ubiquitin-mediated degradation. Enhances the inhibitory activity of SMAD7 and reduces the transcriptional activity of SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable decrease in steady-state level of SMAD1 protein and a smaller decrease of SMAD2 level.[1][2]

About this Structure

2kxq is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

  • Chong PA, Lin H, Wrana JL, Forman-Kay JD. Coupling of tandem Smad ubiquitination regulatory factor (Smurf) WW domains modulates target specificity. Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18404-9. Epub 2010 Oct 11. PMID:20937913 doi:10.1073/pnas.1003023107
  1. Bonni S, Wang HR, Causing CG, Kavsak P, Stroschein SL, Luo K, Wrana JL. TGF-beta induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradation. Nat Cell Biol. 2001 Jun;3(6):587-95. PMID:11389444 doi:10.1038/35078562
  2. Di Guglielmo GM, Le Roy C, Goodfellow AF, Wrana JL. Distinct endocytic pathways regulate TGF-beta receptor signalling and turnover. Nat Cell Biol. 2003 May;5(5):410-21. PMID:12717440 doi:10.1038/ncb975

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools