2v5y: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
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]. | 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]. | ||
==Reference== | ==Reference== | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
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Revision as of 11:49, 3 February 2008
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CRYSTAL STRUCTURE OF THE RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU ECTODOMAIN
OverviewOverview
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 StructureAbout this Structure
2V5Y is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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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OCA- Pages with broken file links
- Homo sapiens
- Protein-tyrosine-phosphatase
- Single protein
- Aricescu, A.R.
- Chang, V.T.
- Choudhuri, K.
- Davis, S.J.
- Jones, E.Y.
- Lu, W.
- Merwe, P.A.Van.Der.
- Siebold, C.
- NA
- NAG
- Cell adhesion
- Extracellular region
- Glycoprotein
- Hydrolase
- Immunoglobulin domain
- Membrane
- Protein phosphatase
- Receptor
- Receptor protein tyrosine phosphatase
- Transmembrane