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| | <StructureSection load='2c9a' size='340' side='right'caption='[[2c9a]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='2c9a' size='340' side='right'caption='[[2c9a]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2c9a]] 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=2C9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C9A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2c9a]] is a 1 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=2C9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C9A FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rpm|1rpm]]</div></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'>[https://proteopedia.org/fgij/fg.htm?mol=2c9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9a OCA], [https://pdbe.org/2c9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c9a RCSB], [https://www.ebi.ac.uk/pdbsum/2c9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c9a 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=2c9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9a OCA], [https://pdbe.org/2c9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c9a RCSB], [https://www.ebi.ac.uk/pdbsum/2c9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c9a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PTPRM_HUMAN PTPRM_HUMAN]] Involved in cell-cell adhesion through homophilic interactions. May play a key role in signal transduction and growth control.<ref>PMID:16456543</ref>
| + | [https://www.uniprot.org/uniprot/PTPRM_HUMAN PTPRM_HUMAN] Involved in cell-cell adhesion through homophilic interactions. May play a key role in signal transduction and growth control.<ref>PMID:16456543</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Protein-tyrosine-phosphatase]]
| + | [[Category: Aricescu AR]] |
| - | [[Category: Aricescu, A R]] | + | [[Category: Hon WC]] |
| - | [[Category: Hon, W C]] | + | [[Category: Jones EY]] |
| - | [[Category: Jones, E Y]] | + | [[Category: Lu W]] |
| - | [[Category: Lu, W]] | + | [[Category: Siebold C]] |
| - | [[Category: Merwe, P A.Van Der]]
| + | [[Category: Van Der Merwe PA]] |
| - | [[Category: Siebold, C]] | + | |
| - | [[Category: Glycoprotein]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Immunoglobulin domain]]
| + | |
| - | [[Category: Receptor]]
| + | |
| Structural highlights
2c9a is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.7Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
PTPRM_HUMAN Involved in cell-cell adhesion through homophilic interactions. May play a key role in signal transduction and growth control.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Type IIB receptor protein tyrosine phosphatases (RPTPs) are bi-functional cell surface molecules. Their ectodomains mediate stable, homophilic, cell-adhesive interactions, whereas the intracellular catalytic regions can modulate the phosphorylation state of cadherin/catenin complexes. We describe a systematic investigation of the cell-adhesive properties of the extracellular region of RPTPmu, a prototypical type IIB RPTP. The crystal structure of a construct comprising its N-terminal MAM (meprin/A5/mu) and Ig domains was determined at 2.7 A resolution; this assigns the MAM fold to the jelly-roll family and reveals extensive interactions between the two domains, which form a rigid structural unit. Structure-based site-directed mutagenesis, serial domain deletions and cell-adhesion assays allowed us to identify the four N-terminal domains (MAM, Ig, fibronectin type III (FNIII)-1 and FNIII-2) as a minimal functional unit. Biophysical characterization revealed at least two independent types of homophilic interaction which, taken together, suggest that there is the potential for formation of a complex and possibly ordered array of receptor molecules at cell contact sites.
Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion.,Aricescu AR, Hon WC, Siebold C, Lu W, van der Merwe PA, Jones EY EMBO J. 2006 Feb 22;25(4):701-12. Epub 2006 Feb 2. PMID:16456543[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Aricescu AR, Hon WC, Siebold C, Lu W, van der Merwe PA, Jones EY. Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion. EMBO J. 2006 Feb 22;25(4):701-12. Epub 2006 Feb 2. PMID:16456543
- ↑ Aricescu AR, Hon WC, Siebold C, Lu W, van der Merwe PA, Jones EY. Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion. EMBO J. 2006 Feb 22;25(4):701-12. Epub 2006 Feb 2. PMID:16456543
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