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2c9a

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[[Image:2c9a.gif|left|200px]]<br />
 
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<applet load="2c9a" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2c9a, resolution 2.70&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE MAM-IG MODULE OF RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU'''<br />
 
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==Overview==
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==Crystal structure of the MAM-Ig module of receptor protein tyrosine phosphatase mu==
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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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?16456543 (full description)]]
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<StructureSection load='2c9a' size='340' side='right'caption='[[2c9a]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/2c9a_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2c9a ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:16456543</ref>
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2C9A is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with NAG and NA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C9A OCA]].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16456543 16456543]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 2c9a" style="background-color:#fffaf0;"></div>
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[[Category: Protein-tyrosine-phosphatase]]
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[[Category: Single protein]]
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[[Category: Aricescu, A.R.]]
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[[Category: Hon, W.C.]]
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[[Category: Jones, E.Y.]]
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[[Category: Lu, W.]]
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[[Category: Merwe, P.A.Van.Der.]]
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[[Category: Siebold, C.]]
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[[Category: NA]]
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[[Category: NAG]]
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[[Category: glycoprotein]]
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[[Category: hydrolase]]
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[[Category: immunoglobulin domain]]
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[[Category: receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:03:36 2007''
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==See Also==
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*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Aricescu AR]]
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[[Category: Hon WC]]
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[[Category: Jones EY]]
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[[Category: Lu W]]
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[[Category: Siebold C]]
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[[Category: Van Der Merwe PA]]

Current revision

Crystal structure of the MAM-Ig module of receptor protein tyrosine phosphatase mu

PDB ID 2c9a

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