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==Crystal structures of FNIII domain three and four of the human leucocyte common antigen-related protein, LAR== | ==Crystal structures of FNIII domain three and four of the human leucocyte common antigen-related protein, LAR== | ||
<StructureSection load='6tpu' size='340' side='right'caption='[[6tpu]]' scene=''> | <StructureSection load='6tpu' size='340' side='right'caption='[[6tpu]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TPU OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6tpu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TPU FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=6tpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tpu OCA], [https://pdbe.org/6tpu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tpu RCSB], [https://www.ebi.ac.uk/pdbsum/6tpu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tpu ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://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> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Leucocyte common antigen-related protein (LAR) is a post-synaptic type I transmembrane receptor protein that is important for neuronal functionality and is genetically coupled to neuronal disorders such as attention deficit hyperactivity disorder (ADHD). To understand the molecular function of LAR, structural and biochemical studies of protein fragments derived from the ectodomain of human LAR have been performed. The crystal structure of a fragment encompassing the first four FNIII domains (LAR(FN1-4)) showed a characteristic L shape. SAXS data suggested limited flexibility within LAR(FN1-4), while rigid-body refinement of the SAXS data using the X-ray-derived atomic model showed a smaller angle between the domains defining the L shape compared with the crystal structure. The capabilities of the individual LAR fragments to interact with heparin was examined using microscale thermophoresis and heparin-affinity chromatography. The results showed that the three N-terminal immunoglobulin domains (LAR(Ig1-3)) and the four C-terminal FNIII domains (LAR(FN5-8)) both bound heparin, while LAR(FN1-4) did not. The low-molecular-weight heparin drug Innohep induced a shift in hydrodynamic volume as assessed by size-exclusion chromatography of LAR(Ig1-3) and LAR(FN5-8), while the chemically defined pentameric heparin drug Arixtra did not. Together, the presented results suggest the presence of an additional heparin-binding site in human LAR. | |||
Crystal and solution structures of fragments of the human leucocyte common antigen-related protein.,Vilstrup J, Simonsen A, Birkefeldt T, Strandbygard D, Lyngso J, Pedersen JS, Thirup S Acta Crystallogr D Struct Biol. 2020 May 1;76(Pt 5):406-417. doi:, 10.1107/S2059798320003885. Epub 2020 Apr 15. PMID:32355037<ref>PMID:32355037</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6tpu" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Birkefeldt T]] | [[Category: Birkefeldt T]] | ||
Latest revision as of 16:07, 24 January 2024
Structural highlights
FunctionPTPRF_HUMAN Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase).[1] The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one.[2] Publication Abstract from PubMedLeucocyte common antigen-related protein (LAR) is a post-synaptic type I transmembrane receptor protein that is important for neuronal functionality and is genetically coupled to neuronal disorders such as attention deficit hyperactivity disorder (ADHD). To understand the molecular function of LAR, structural and biochemical studies of protein fragments derived from the ectodomain of human LAR have been performed. The crystal structure of a fragment encompassing the first four FNIII domains (LAR(FN1-4)) showed a characteristic L shape. SAXS data suggested limited flexibility within LAR(FN1-4), while rigid-body refinement of the SAXS data using the X-ray-derived atomic model showed a smaller angle between the domains defining the L shape compared with the crystal structure. The capabilities of the individual LAR fragments to interact with heparin was examined using microscale thermophoresis and heparin-affinity chromatography. The results showed that the three N-terminal immunoglobulin domains (LAR(Ig1-3)) and the four C-terminal FNIII domains (LAR(FN5-8)) both bound heparin, while LAR(FN1-4) did not. The low-molecular-weight heparin drug Innohep induced a shift in hydrodynamic volume as assessed by size-exclusion chromatography of LAR(Ig1-3) and LAR(FN5-8), while the chemically defined pentameric heparin drug Arixtra did not. Together, the presented results suggest the presence of an additional heparin-binding site in human LAR. Crystal and solution structures of fragments of the human leucocyte common antigen-related protein.,Vilstrup J, Simonsen A, Birkefeldt T, Strandbygard D, Lyngso J, Pedersen JS, Thirup S Acta Crystallogr D Struct Biol. 2020 May 1;76(Pt 5):406-417. doi:, 10.1107/S2059798320003885. Epub 2020 Apr 15. PMID:32355037[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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