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2yd1

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Revision as of 12:26, 27 April 2022

Crystal structure of the N-terminal Ig1-2 module of Drosophila Receptor Protein Tyrosine Phosphatase DLAR

Structural highlights

2yd1 is a 1 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2yd6, 2yd7, 2yd8, 2yd5, 2yd2, 2yd4, 2yd9, 2yd3
Activity:	Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LAR_DROME] Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase). It controls motor axon guidance.^[1] ^[2]

Publication Abstract from PubMed

Heparan and chondroitin sulfate proteoglycans (HSPGs and CSPGs) regulate numerous cell surface signaling events, with typically opposite effects on cell function. CSPGs inhibit nerve regeneration through receptor protein tyrosine phosphatase sigma (RPTPsigma). Here, we report that RPTPsigma acts bimodally in sensory neuron extension, mediating CSPG inhibition and HSPG growth promotion. Crystallographic analyses of a shared HSPG-CSPG binding site reveal a conformational plasticity that can accommodate diverse glycosaminoglycans with comparable affinities. Heparan sulfate and analogues induced RPTPsigma ectodomain oligomerization in solution, which chondroitin sulfate inhibited. RPTPsigma and HSPGs colocalize in puncta on sensory neurons in culture, whereas CSPGs occupy the extracellular matrix. These results lead to a model where proteoglycans can exert opposing effects on neuronal extension by competing to control the oligomerization of a common receptor.

Proteoglycan-Specific Molecular Switch for RPTP{sigma} Clustering and Neuronal Extension.,Coles CH, Shen Y, Tenney AP, Siebold C, Sutton GC, Lu W, Gallagher JT, Jones EY, Flanagan JG, Aricescu AR Science. 2011 Mar 31. PMID:21454754^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Streuli M, Krueger NX, Tsai AY, Saito H. A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila. Proc Natl Acad Sci U S A. 1989 Nov;86(22):8698-702. PMID:2554325
↑ Krueger NX, Van Vactor D, Wan HI, Gelbart WM, Goodman CS, Saito H. The transmembrane tyrosine phosphatase DLAR controls motor axon guidance in Drosophila. Cell. 1996 Feb 23;84(4):611-22. PMID:8598047
↑ Coles CH, Shen Y, Tenney AP, Siebold C, Sutton GC, Lu W, Gallagher JT, Jones EY, Flanagan JG, Aricescu AR. Proteoglycan-Specific Molecular Switch for RPTP{sigma} Clustering and Neuronal Extension. Science. 2011 Mar 31. PMID:21454754 doi:10.1126/science.1200840

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2yd1"

@@ Line 3: / Line 3: @@
 <StructureSection load='2yd1' size='340' side='right'caption='[[2yd1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2yd1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YD1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2YD1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2yd1]] is a 1 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=2YD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YD1 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yd6|2yd6]], [[2yd7|2yd7]], [[2yd8|2yd8]], [[2yd5|2yd5]], [[2yd2|2yd2]], [[2yd4|2yd4]], [[2yd9|2yd9]], [[2yd3|2yd3]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2yd6|2yd6]], [[2yd7|2yd7]], [[2yd8|2yd8]], [[2yd5|2yd5]], [[2yd2|2yd2]], [[2yd4|2yd4]], [[2yd9|2yd9]], [[2yd3|2yd3]]</div></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='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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2yd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yd1 OCA], [http://pdbe.org/2yd1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yd1 RCSB], [http://www.ebi.ac.uk/pdbsum/2yd1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yd1 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=2yd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yd1 OCA], [https://pdbe.org/2yd1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yd1 RCSB], [https://www.ebi.ac.uk/pdbsum/2yd1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yd1 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2yd1

From Proteopedia

Revision as of 12:26, 27 April 2022

Crystal structure of the N-terminal Ig1-2 module of Drosophila Receptor Protein Tyrosine Phosphatase DLAR

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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