2c9a: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,329,557 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,329,557 edits
No edit summary
 
(14 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2c9a.jpg|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_2c9a", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_2c9a|  PDB=2c9a  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF THE MAM-IG MODULE OF RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU'''


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


==Overview==
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>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2C9A is a [[Single protein]] structure of sequence from [http://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].
</div>
<div class="pdbe-citations 2c9a" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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://www.ncbi.nlm.nih.gov/pubmed/16456543 16456543]
*[[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: Glycoprotein]]
[[Category: Hydrolase]]
[[Category: Immunoglobulin domain]]
[[Category: Receptor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 21:29:43 2008''

Latest revision as of 07:48, 23 October 2024

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

2c9a, resolution 2.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2c9a&oldid=4234647"