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6kr4
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the liprin-alpha3_SAM123/LAR_D1D2 complex== | |
| + | <StructureSection load='6kr4' size='340' side='right'caption='[[6kr4]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6kr4]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [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=6KR4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KR4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPRF, LAR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), Ppfia3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></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=6kr4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kr4 OCA], [http://pdbe.org/6kr4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kr4 RCSB], [http://www.ebi.ac.uk/pdbsum/6kr4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kr4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PTPRF_HUMAN PTPRF_HUMAN]] Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase).<ref>PMID:10338209</ref> The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one.<ref>PMID:10338209</ref> [[http://www.uniprot.org/uniprot/LIPA3_MOUSE LIPA3_MOUSE]] May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Leukocyte common antigen-related receptor protein tyrosine phosphatases (LAR-RPTPs) are cell adhesion molecules involved in mediating neuronal development. The binding of LAR-RPTPs to extracellular ligands induces local clustering of LAR-RPTPs to regulate axon growth and synaptogenesis. LAR-RPTPs interact with synaptic liprin-alpha proteins via the two cytoplasmic phosphatase domains, D1 and D2. Here we solve the crystal structure of LAR_D1D2 in complex with the SAM repeats of liprin-alpha3, uncovering a conserved two-site binding mode. Cellular analysis shows that liprin-alphas robustly promote clustering of LAR in cells by both the liprin-alpha/LAR interaction and the oligomerization of liprin-alpha. Structural analysis reveals a unique homophilic interaction of LAR via the catalytically active D1 domains. Disruption of the D1/D1 interaction diminishes the liprin-alpha-promoted LAR clustering and increases tyrosine dephosphorylation, demonstrating that the phosphatase activity of LAR is negatively regulated by forming clusters. Additionally, we find that the binding of LAR to liprin-alpha allosterically regulates the liprin-alpha/liprin-beta interaction. | ||
| - | + | Structural basis of liprin-alpha-promoted LAR-RPTP clustering for modulation of phosphatase activity.,Xie X, Luo L, Liang M, Zhang W, Zhang T, Yu C, Wei Z Nat Commun. 2020 Jan 10;11(1):169. doi: 10.1038/s41467-019-13949-x. PMID:31924785<ref>PMID:31924785</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6kr4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lk3 transgenic mice]] | ||
| + | [[Category: Protein-tyrosine-phosphatase]] | ||
| + | [[Category: Liang, M]] | ||
| + | [[Category: Luo, L]] | ||
| + | [[Category: Wei, Z]] | ||
| + | [[Category: Xie, X]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Phosphatase]] | ||
| + | [[Category: Transferase-protein binding complex]] | ||
Revision as of 16:10, 29 January 2020
Crystal structure of the liprin-alpha3_SAM123/LAR_D1D2 complex
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