3pxh: Difference between revisions
New page: '''Unreleased structure''' The entry 3pxh is ON HOLD Authors: Biersmith, B.H., Bouyain, S. Description: Tandem Ig domains of tyrosine phosphatase LAR ''Page seeded by [http://oca.weiz... |
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==Tandem Ig domains of tyrosine phosphatase LAR== | |||
<StructureSection load='3pxh' size='340' side='right'caption='[[3pxh]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3pxh]] 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=3PXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PXH FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.0009Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3pxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pxh OCA], [https://pdbe.org/3pxh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pxh RCSB], [https://www.ebi.ac.uk/pdbsum/3pxh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pxh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3pxh" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Biersmith BH]] | |||
[[Category: Bouyain S]] | |||