|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==Crystal Structure of C-terminal Truncated TIP-1 (6-113)== | | ==Crystal Structure of C-terminal Truncated TIP-1 (6-113)== |
| - | <StructureSection load='3dj3' size='340' side='right' caption='[[3dj3]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='3dj3' size='340' side='right'caption='[[3dj3]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3dj3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DJ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DJ3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3dj3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DJ3 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3diw|3diw]], [[3dj1|3dj1]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dj3 OCA], [http://pdbe.org/3dj3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dj3 RCSB], [http://www.ebi.ac.uk/pdbsum/3dj3 PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dj3 OCA], [https://pdbe.org/3dj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dj3 RCSB], [https://www.ebi.ac.uk/pdbsum/3dj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dj3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TX1B3_MOUSE TX1B3_MOUSE]] May regulate a number of protein-protein interactions by competing for PDZ domain binding sites. Binds CTNNB1 and may thereby act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play a role in the Rho signaling pathway (By similarity).<ref>PMID:12874278</ref> | + | [https://www.uniprot.org/uniprot/TX1B3_MOUSE TX1B3_MOUSE] May regulate a number of protein-protein interactions by competing for PDZ domain binding sites. Binds CTNNB1 and may thereby act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play a role in the Rho signaling pathway (By similarity).<ref>PMID:12874278</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dj/3dj3_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dj/3dj3_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| Line 31: |
Line 32: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Shen, Y]] | + | [[Category: Mus musculus]] |
| - | [[Category: Nucleus]] | + | [[Category: Shen Y]] |
| - | [[Category: Pdz domain]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Tip-1]]
| + | |
| - | [[Category: Wnt signaling pathway]]
| + | |
| Structural highlights
Function
TX1B3_MOUSE May regulate a number of protein-protein interactions by competing for PDZ domain binding sites. Binds CTNNB1 and may thereby act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play a role in the Rho signaling pathway (By similarity).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Tax-interacting protein-1 (TIP-1) is an unusual signaling protein, containing a single PDZ domain. TIP-1 is able to bind beta-catenin with high affinity and thus inhibit its transcriptional activity. The high-resolution crystal structure of TIP-1 in complex with the C-terminal peptide of beta-catenin provides molecular details for the recognition of beta-catenin by TIP-1. Moreover, structural comparison of peptide-free and peptide-bound TIP-1 reveals that significant conformational changes are required in the betaB-betaC loop region of TIP-1 to avoid clashes with the incoming C-terminal beta-catenin peptide. Such conformational changes have not been observed in other structures of PDZ domains. In addition to the canonical peptide-binding pocket of the PDZ domain, TIP-1 can form a binding cavity to anchor more amino acids through a conserved hydrophobic residue pair (Trp776 of beta-catenin and Pro45 of TIP-1). Structural and biochemical data indicate that the canonical binding pocket together with the hydrophobic residue pair are presumably the major cause of the significantly higher affinity of the beta-catenin C-terminal to TIP-1 than to other PDZ domains, providing a unique binding specificity. Our results reveal the molecular mechanism of TIP-1 as an antagonist in PDZ domain signaling.
Structural basis of beta-catenin recognition by Tax-interacting protein-1.,Zhang J, Yan X, Shi C, Yang X, Guo Y, Tian C, Long J, Shen Y J Mol Biol. 2008 Dec 5;384(1):255-63. Epub 2008 Sep 21. PMID:18835279[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kanamori M, Sandy P, Marzinotto S, Benetti R, Kai C, Hayashizaki Y, Schneider C, Suzuki H. The PDZ protein tax-interacting protein-1 inhibits beta-catenin transcriptional activity and growth of colorectal cancer cells. J Biol Chem. 2003 Oct 3;278(40):38758-64. Epub 2003 Jul 21. PMID:12874278 doi:10.1074/jbc.M306324200
- ↑ Zhang J, Yan X, Shi C, Yang X, Guo Y, Tian C, Long J, Shen Y. Structural basis of beta-catenin recognition by Tax-interacting protein-1. J Mol Biol. 2008 Dec 5;384(1):255-63. Epub 2008 Sep 21. PMID:18835279 doi:10.1016/j.jmb.2008.09.034
|
