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6x39

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Current revision (07:10, 3 April 2024) (edit) (undo)
 
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<StructureSection load='6x39' size='340' side='right'caption='[[6x39]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='6x39' size='340' side='right'caption='[[6x39]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6x39]] is a 1 chain structure with sequence from [https://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=6X39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X39 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6x39]] is a 1 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=6X39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X39 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SOR:D-SORBITOL'>SOR</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ptprf, Lar ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SOR:D-SORBITOL'>SOR</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6x39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x39 OCA], [https://pdbe.org/6x39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x39 RCSB], [https://www.ebi.ac.uk/pdbsum/6x39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x39 ProSAT]</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=6x39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x39 OCA], [https://pdbe.org/6x39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x39 RCSB], [https://www.ebi.ac.uk/pdbsum/6x39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x39 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PTPRF_MOUSE PTPRF_MOUSE]] Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity (By similarity).
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[https://www.uniprot.org/uniprot/PTPRF_MOUSE PTPRF_MOUSE] Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The type IIa family of receptor protein tyrosine phosphatases (RPTPs), including Lar, RPTPsigma and RPTPdelta, are well-studied in coordinating actin cytoskeletal rearrangements during axon guidance and synaptogenesis. To determine whether this regulation is conserved in other tissues, interdisciplinary approaches were utilized to study Lar-RPTPs in the Drosophila musculature. Here we find that the single fly ortholog, Drosophila Lar (Dlar), is localized to the muscle costamere and that a decrease in Dlar causes aberrant sarcomeric patterning, deficits in larval locomotion, and integrin mislocalization. Sequence analysis uncovered an evolutionarily conserved Lys-Gly-Asp (KGD) signature in the extracellular region of Dlar. Since this tripeptide sequence is similar to the integrin-binding Arg-Gly-Asp (RGD) motif, we tested the hypothesis that Dlar directly interacts with integrin proteins. However, structural analyses of the fibronectin type III domains of Dlar and two vertebrate orthologs that include this conserved motif indicate that this KGD tripeptide is not accessible and thus unlikely to mediate physical interactions with integrins. These results, together with the proteomics identification of basement membrane (BM) proteins as potential ligands for type IIa RPTPs, suggest a complex network of protein interactions in the extracellular space that may mediate Lar function and/or signaling in muscle tissue.
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Complex protein interactions mediate Drosophila Lar function in muscle tissue.,Kawakami J, Brooks D, Zalmai R, Hartson SD, Bouyain S, Geisbrecht ER PLoS One. 2022 May 27;17(5):e0269037. doi: 10.1371/journal.pone.0269037., eCollection 2022. PMID:35622884<ref>PMID:35622884</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6x39" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Protein-tyrosine-phosphatase]]
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[[Category: Bouyain S]]
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[[Category: Bouyain, S]]
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[[Category: Kawakami JE]]
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[[Category: Kawakami, J E]]
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[[Category: Cell adhesion]]
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[[Category: Fibronectin type iii]]
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[[Category: Receptor protein tyrosine phosphatase]]
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Current revision

Crystal structure of the FN5 domain of Mouse Lar

PDB ID 6x39

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