2v5y: Difference between revisions
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|PDB= 2v5y |SIZE=350|CAPTION= <scene name='initialview01'>2v5y</scene>, resolution 3.10Å | |PDB= 2v5y |SIZE=350|CAPTION= <scene name='initialview01'>2v5y</scene>, resolution 3.10Å | ||
|SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
|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] | |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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1rpm|1RPM]], [[2c9a|2C9A]] | |||
|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> | |||
}} | }} | ||
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[[Category: Merwe, P A.Van Der.]] | [[Category: Merwe, P A.Van Der.]] | ||
[[Category: Siebold, C.]] | [[Category: Siebold, C.]] | ||
[[Category: cell adhesion]] | [[Category: cell adhesion]] | ||
[[Category: extracellular region]] | [[Category: extracellular region]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:08:36 2008'' | ||
Revision as of 05:08, 31 March 2008
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| , resolution 3.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Protein-tyrosine-phosphatase, with EC number 3.1.3.48 | ||||||
| Related: | 1RPM, 2C9A
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Mon Mar 31 05:08:36 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
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.
- Cell adhesion
- Extracellular region
- Glycoprotein
- Hydrolase
- Immunoglobulin domain
- Membrane
- Protein phosphatase
- Receptor
- Receptor protein tyrosine phosphatase
- Transmembrane