2c9a: Difference between revisions

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[[Image:2c9a.gif|left|200px]]<br />
<applet load="2c9a" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2c9a, resolution 2.70&Aring;" />
'''CRYSTAL STRUCTURE OF THE MAM-IG MODULE OF RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU'''<br />


==Overview==
==Crystal structure of the MAM-Ig module of receptor protein tyrosine phosphatase mu==
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.
<StructureSection load='2c9a' size='340' side='right'caption='[[2c9a]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<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='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>
<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='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>
== 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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/2c9a_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==About this Structure==
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>
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].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
<div class="pdbe-citations 2c9a" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[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: NA]]
[[Category: NAG]]
[[Category: glycoprotein]]
[[Category: hydrolase]]
[[Category: immunoglobulin domain]]
[[Category: receptor]]
 
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Retrieved from "https://proteopedia.org/2c9a"