2v5y

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[[Image:2v5y.jpg|left|200px]]<br /><applet load="2v5y" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2v5y.jpg|left|200px]]
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caption="2v5y, resolution 3.10&Aring;" />
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'''CRYSTAL STRUCTURE OF THE RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU ECTODOMAIN'''<br />
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{{Structure
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|PDB= 2v5y |SIZE=350|CAPTION= <scene name='initialview01'>2v5y</scene>, resolution 3.10&Aring;
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|SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF THE RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU ECTODOMAIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2V5Y 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 <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=NA:'>NA</scene> 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] Known structural/functional Site: <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5Y OCA].
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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].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17761881 17761881]
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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: Protein-tyrosine-phosphatase]]
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[[Category: transmembrane]]
[[Category: transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:53:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:43:22 2008''

Revision as of 16:43, 20 March 2008

Image:2v5y.jpg


PDB ID 2v5y

Drag the structure with the mouse to rotate
, resolution 3.10Å
Sites:
Ligands: and
Activity: Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU ECTODOMAIN


Overview

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.

About this Structure

2V5Y is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

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:17761881

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