2ltx
From Proteopedia
(Difference between revisions)
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==Smurf1 WW2 domain in complex with a Smad7 derived peptide== | ==Smurf1 WW2 domain in complex with a Smad7 derived peptide== | ||
- | <StructureSection load='2ltx' size='340' side='right' caption='[[2ltx]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | + | <StructureSection load='2ltx' size='340' side='right'caption='[[2ltx]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2ltx]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2ltx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LTX FirstGlance]. <br> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ltv|2ltv]], [[2ltw|2ltw]], [[2lty|2lty]], [[2ltz|2ltz]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ltv|2ltv]], [[2ltw|2ltw]], [[2lty|2lty]], [[2ltz|2ltz]]</div></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMURF1, KIAA1625 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMURF1, KIAA1625 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ltx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ltx OCA], [https://pdbe.org/2ltx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ltx RCSB], [https://www.ebi.ac.uk/pdbsum/2ltx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ltx ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == Disease == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/SMAD7_HUMAN SMAD7_HUMAN]] Genetic variations in SMAD7 influence susceptibility to colorectal cancer type 3 (CRCS3) [MIM:[https://omim.org/entry/612229 612229]]. Colorectal cancer consists of tumors or cancer of either the colon or rectum or both. Cancers of the large intestine are the second most common form of cancer found in males and females. Symptoms include rectal bleeding, occult blood in stools, bowel obstruction and weight loss. Treatment is based largely on the extent of cancer penetration into the intestinal wall. Surgical cures are possible if the malignancy is confined to the intestine. Risk can be reduced when following a diet which is low in fat and high in fiber.<ref>PMID:17934461</ref> |
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/SMUF1_HUMAN SMUF1_HUMAN]] E3 ubiquitin-protein ligase that acts as a negative regulator of BMP signaling pathway. Mediates ubiquitination and degradation of SMAD1 and SMAD5, 2 receptor-regulated SMADs specific for the BMP pathway. Promotes ubiquitination and subsequent proteasomal degradation of TRAF family members and RHOA.<ref>PMID:10458166</ref> <ref>PMID:19937093</ref> <ref>PMID:21402695</ref> [[https://www.uniprot.org/uniprot/SMAD7_HUMAN SMAD7_HUMAN]] Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator (By similarity).<ref>PMID:9892009</ref> <ref>PMID:11163210</ref> <ref>PMID:12023024</ref> <ref>PMID:14718519</ref> <ref>PMID:17327236</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
- | *[[Ubiquitin protein ligase|Ubiquitin protein ligase]] | + | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Aragon, E]] | [[Category: Aragon, E]] | ||
[[Category: Gao, S]] | [[Category: Gao, S]] |
Revision as of 10:53, 19 May 2021
Smurf1 WW2 domain in complex with a Smad7 derived peptide
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Categories: Human | Large Structures | Aragon, E | Gao, S | Goerner, N | Lopes, T | Macias, M J | Massague, J | Xi, Q | Protein binding-peptide complex | Smad7 | Smurf1 | Ww