2V5Y

Crystal structure of the receptor protein tyrosine phosphatase mu ectodomain

Summary for 2V5Y

• Entry DOI: 10.2210/pdb2v5y/pdb
• Related: 1RPM 2C9A
• Descriptor: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE MU, 2-acetamido-2-deoxy-beta-D-glucopyranose, SODIUM ION (3 entities in total)
• Functional Keywords: membrane, receptor, hydrolase, glycoprotein, receptor protein tyrosine phosphatase, cell adhesion, transmembrane, protein phosphatase, extracellular region, immunoglobulin domain
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 83293.78

Authors

Aricescu, A.R.,Siebold, C.,Choudhuri, K.,Chang, V.T.,Lu, W.,Davis, S.J.,van der Merwe, P.A.,Jones, E.Y. (deposition date: 2007-07-11, release date: 2007-09-11, Last modification date: 2024-11-20)

Primary citation

Aricescu, A.R.,Siebold, C.,Choudhuri, K.,Chang, V.T.,Lu, W.,Davis, S.J.,Van Der Merwe, P.A.,Jones, E.Y.
Structure of a Tyrosine Phosphatase Adhesive Interaction Reveals a Spacer-Clamp Mechanism.
Science, 317:1217-, 2007

PubMed Abstract: 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.

PubMed: 17761881
DOI: 10.1126/SCIENCE.1144646

Experimental method

X-RAY DIFFRACTION (3.1 Å)