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2yd5

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Revision as of 12:27, 27 April 2022

Crystal structure of the N-terminal Ig1-2 module of Human Receptor Protein Tyrosine Phosphatase LAR

Structural highlights

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

Function

[PTPRF_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 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

↑ Nam HJ, Poy F, Krueger NX, Saito H, Frederick CA. Crystal structure of the tandem phosphatase domains of RPTP LAR. Cell. 1999 May 14;97(4):449-57. PMID:10338209
↑ Nam HJ, Poy F, Krueger NX, Saito H, Frederick CA. Crystal structure of the tandem phosphatase domains of RPTP LAR. Cell. 1999 May 14;97(4):449-57. PMID:10338209
↑ 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/2yd5"

@@ Line 3: / Line 3: @@
 <StructureSection load='2yd5' size='340' side='right'caption='[[2yd5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2yd5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YD5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2YD5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2yd5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YD5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YD5 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lar|1lar]], [[2yd6|2yd6]], [[2yd7|2yd7]], [[2yd1|2yd1]], [[2yd8|2yd8]], [[2yd2|2yd2]], [[2yd4|2yd4]], [[2yd9|2yd9]], [[2yd3|2yd3]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1lar|1lar]], [[2yd6|2yd6]], [[2yd7|2yd7]], [[2yd1|2yd1]], [[2yd8|2yd8]], [[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=2yd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yd5 OCA], [http://pdbe.org/2yd5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yd5 RCSB], [http://www.ebi.ac.uk/pdbsum/2yd5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yd5 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=2yd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yd5 OCA], [https://pdbe.org/2yd5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yd5 RCSB], [https://www.ebi.ac.uk/pdbsum/2yd5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yd5 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[[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 ==

2yd5

From Proteopedia

Revision as of 12:27, 27 April 2022

Crystal structure of the N-terminal Ig1-2 module of Human Receptor Protein Tyrosine Phosphatase LAR

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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