2v5y: Difference between revisions

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[[Image:2v5y.jpg|left|200px]]


{{Structure
==Crystal structure of the receptor protein tyrosine phosphatase mu ectodomain==
|PDB= 2v5y |SIZE=350|CAPTION= <scene name='initialview01'>2v5y</scene>, resolution 3.10&Aring;
<StructureSection load='2v5y' size='340' side='right'caption='[[2v5y]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
<table><tr><td colspan='2'>[[2v5y]] 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=2V5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V5Y FirstGlance]. <br>
|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
|GENE=
<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></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v5y OCA], [https://pdbe.org/2v5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v5y RCSB], [https://www.ebi.ac.uk/pdbsum/2v5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v5y ProSAT]</span></td></tr>
|RELATEDENTRY=[[1rpm|1RPM]], [[2c9a|2C9A]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v5y OCA], [http://www.ebi.ac.uk/pdbsum/2v5y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v5y RCSB]</span>
== 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/v5/2v5y_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=2v5y ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cell-cell contacts are fundamental to multicellular organisms and are subject to exquisite levels of control. Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes. Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions. Cell surface expression of deletion constructs induces intercellular spacings that correlate with the ectodomain length. These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.


'''CRYSTAL STRUCTURE OF THE RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU ECTODOMAIN'''
Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism.,Aricescu AR, Siebold C, Choudhuri K, Chang VT, Lu W, Davis SJ, van der Merwe PA, Jones EY Science. 2007 Aug 31;317(5842):1217-20. PMID:17761881<ref>PMID:17761881</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2v5y" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Cell-cell contacts are fundamental to multicellular organisms and are subject to exquisite levels of control. Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes. Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions. Cell surface expression of deletion constructs induces intercellular spacings that correlate with the ectodomain length. These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.
*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
 
== References ==
==About this Structure==
<references/>
2V5Y 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=2V5Y OCA].
__TOC__
 
</StructureSection>
==Reference==
Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism., Aricescu AR, Siebold C, Choudhuri K, Chang VT, Lu W, Davis SJ, van der Merwe PA, Jones EY, Science. 2007 Aug 31;317(5842):1217-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17761881 17761881]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Aricescu AR]]
[[Category: Aricescu, A R.]]
[[Category: Chang VT]]
[[Category: Chang, V T.]]
[[Category: Choudhuri K]]
[[Category: Choudhuri, K.]]
[[Category: Davis SJ]]
[[Category: Davis, S J.]]
[[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: cell adhesion]]
[[Category: extracellular region]]
[[Category: glycoprotein]]
[[Category: hydrolase]]
[[Category: immunoglobulin domain]]
[[Category: membrane]]
[[Category: protein phosphatase]]
[[Category: receptor]]
[[Category: receptor protein tyrosine phosphatase]]
[[Category: transmembrane]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:08:36 2008''

Latest revision as of 04:26, 21 November 2024

Crystal structure of the receptor protein tyrosine phosphatase mu ectodomainCrystal structure of the receptor protein tyrosine phosphatase mu ectodomain

Structural highlights

2v5y 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 3.1Å
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

Cell-cell contacts are fundamental to multicellular organisms and are subject to exquisite levels of control. Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes. Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions. Cell surface expression of deletion constructs induces intercellular spacings that correlate with the ectodomain length. These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.

Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism.,Aricescu AR, Siebold C, Choudhuri K, Chang VT, Lu W, Davis SJ, van der Merwe PA, Jones EY Science. 2007 Aug 31;317(5842):1217-20. PMID:17761881[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ 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
  2. ↑ Aricescu AR, Siebold C, Choudhuri K, Chang VT, Lu W, Davis SJ, van der Merwe PA, Jones EY. Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism. Science. 2007 Aug 31;317(5842):1217-20. PMID:17761881 doi:317/5842/1217

2v5y, resolution 3.10Å

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