3pxj

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<StructureSection load='3pxj' size='340' side='right'caption='[[3pxj]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3pxj' size='340' side='right'caption='[[3pxj]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3pxj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PXJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PXJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3pxj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PXJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PXJ FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3px4|3px4]]</div></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]] 2.3003&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Lar, CG10443 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=3pxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pxj OCA], [https://pdbe.org/3pxj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pxj RCSB], [https://www.ebi.ac.uk/pdbsum/3pxj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pxj 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=3pxj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pxj OCA], [https://pdbe.org/3pxj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pxj RCSB], [https://www.ebi.ac.uk/pdbsum/3pxj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pxj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/LAR_DROME LAR_DROME]] Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase). It controls motor axon guidance.<ref>PMID:2554325</ref> <ref>PMID:8598047</ref>
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[https://www.uniprot.org/uniprot/LAR_DROME LAR_DROME] Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase). It controls motor axon guidance.<ref>PMID:2554325</ref> <ref>PMID:8598047</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Neurogenesis depends on exquisitely regulated interactions between macromolecules on the cell surface and in the extracellular matrix. In particular, interactions between proteoglycans and members of the type IIa subgroup of receptor protein tyrosine phosphatases underlie crucial developmental processes such as the formation of synapses at the neuromuscular junction and the migration of axons to their appropriate targets. We report the crystal structures of the first and second immunoglobulin-like domains of the Drosophila type IIa receptor Dlar and its mouse homolog LAR. These two domains adopt an unusual antiparallel arrangement that has not been reported in tandem repeats of immunoglobulin-like domains and that is presumably conserved in all type IIa receptor protein tyrosine phosphatases.
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The Immunoglobulin-like Domains 1 and 2 of the Protein Tyrosine Phosphatase LAR Adopt an Unusual Horseshoe-like Conformation.,Biersmith BH, Hammel M, Geisbrecht ER, Bouyain S J Mol Biol. 2011 May 13;408(4):616-27. Epub 2011 Mar 21. PMID:21402080<ref>PMID:21402080</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 3pxj" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Drome]]
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[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Protein-tyrosine-phosphatase]]
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[[Category: Biersmith BH]]
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[[Category: Biersmith, B H]]
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[[Category: Bouyain S]]
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[[Category: Bouyain, S]]
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[[Category: Cell adhesion]]
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[[Category: Hydrolase]]
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[[Category: Ig domain]]
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[[Category: Receptor protein tyrosine phosphatase]]
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Revision as of 13:34, 1 March 2024

Tandem Ig repeats of Dlar

PDB ID 3pxj

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