2l6k
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution Structure of a Nonphosphorylated Peptide Recognizing Domain== | |
| + | <StructureSection load='2l6k' size='340' side='right'caption='[[2l6k]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2l6k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L6K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L6K FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2l6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l6k OCA], [https://pdbe.org/2l6k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l6k RCSB], [https://www.ebi.ac.uk/pdbsum/2l6k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l6k ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TENS2_HUMAN TENS2_HUMAN] Tyrosine-protein phosphatase which regulates cell motility, proliferation and muscle-response to insulin (PubMed:15817639, PubMed:23401856). Phosphatase activity is mediated by binding to phosphatidylinositol-3,4,5-triphosphate (PtdIns(3,4,5)P3) via the SH2 domain (PubMed:30092354). In muscles and under catabolic conditions, dephosphorylates IRS1 leading to its degradation and muscle atrophy (PubMed:23401856, PubMed:30092354). Negatively regulates PI3K-AKT pathway activation (PubMed:15817639, PubMed:23401856, PubMed:30092354). Dephosphorylates nephrin NPHS1 in podocytes which regulates activity of the mTORC1 complex (PubMed:28955049). Under normal glucose conditions, NPHS1 outcompetes IRS1 for binding to phosphatidylinositol 3-kinase (PI3K) which balances mTORC1 activity but high glucose conditions lead to up-regulation of TNS2, increased NPHS1 dephosphorylation and activation of mTORC1, contributing to podocyte hypertrophy and proteinuria (PubMed:28955049). Required for correct podocyte morphology, podocyte-glomerular basement membrane interaction and integrity of the glomerular filtration barrier (By similarity). Enhances RHOA activation in the presence of DLC1 (PubMed:26427649). Plays a role in promoting DLC1-dependent remodeling of the extracellular matrix (PubMed:20069572).[UniProtKB:Q8CGB6]<ref>PMID:15817639</ref> <ref>PMID:20069572</ref> <ref>PMID:23401856</ref> <ref>PMID:26427649</ref> <ref>PMID:28955049</ref> <ref>PMID:30092354</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | BACKGROUND: Src homology 2 (SH2) domain is a conserved module involved in various biological processes. Tensin family member was reported to be involved in tumor suppression by interacting with DLC-1 (deleted-in-liver-cancer-1) via its SH2 domain. We explore here the important questions that what the structure of tensin2 SH2 domain is, and how it binds to DLC-1, which might reveal a novel binding mode. PRINCIPAL FINDINGS: Tensin2 SH2 domain adopts a conserved SH2 fold that mainly consists of five beta-strands flanked by two alpha-helices. Most SH2 domains recognize phosphorylated ligands specifically. However, tensin2 SH2 domain was identified to interact with nonphosphorylated ligand (DLC-1) as well as phosphorylated ligand. CONCLUSIONS: We determined the solution structure of tensin2 SH2 domain using NMR spectroscopy, and revealed the interactions between tensin2 SH2 domain and its ligands in a phosphotyrosine-independent manner. | ||
| - | + | Solution structure of Tensin2 SH2 domain and its phosphotyrosine-independent interaction with DLC-1.,Dai K, Liao S, Zhang J, Zhang X, Tu X PLoS One. 2011;6(7):e21965. Epub 2011 Jul 12. PMID:21765928<ref>PMID:21765928</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2l6k" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Dai K]] | ||
| + | [[Category: Liao S]] | ||
| + | [[Category: Tu X]] | ||
| + | [[Category: Zhang J]] | ||
| + | [[Category: Zhang X]] | ||
Current revision
Solution Structure of a Nonphosphorylated Peptide Recognizing Domain
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Categories: Homo sapiens | Large Structures | Dai K | Liao S | Tu X | Zhang J | Zhang X
