2C9A

Crystal structure of the MAM-Ig module of receptor protein tyrosine phosphatase mu

Summary for 2C9A

• Entry DOI: 10.2210/pdb2c9a/pdb
• Related: 1RPM
• Descriptor: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE MU, alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: glycoprotein, hydrolase, immunoglobulin domain, receptor
• Biological source: HOMO SAPIENS
• Total number of polymer chains: 1
• Total formula weight: 30643.59

Authors

Aricescu, A.R.,Hon, W.C.,Siebold, C.,Lu, W.,Van Der Merwe, P.A.,Jones, E.Y. (deposition date: 2005-12-09, release date: 2006-01-19, Last modification date: 2024-10-23)

Primary citation

Aricescu, A.R.,Hon, W.C.,Siebold, C.,Lu, W.,Van Der Merwe, P.A.,Jones, E.Y.
Molecular Analysis of Receptor Protein Tyrosine Phosphatase Mu-Mediated Cell Adhesion.
Embo J., 25:701-, 2006

PubMed Abstract: Type IIB receptor protein tyrosine phosphatases (RPTPs) are bi-functional cell surface molecules. Their ectodomains mediate stable, homophilic, cell-adhesive interactions, whereas the intracellular catalytic regions can modulate the phosphorylation state of cadherin/catenin complexes. We describe a systematic investigation of the cell-adhesive properties of the extracellular region of RPTPmu, a prototypical type IIB RPTP. The crystal structure of a construct comprising its N-terminal MAM (meprin/A5/mu) and Ig domains was determined at 2.7 A resolution; this assigns the MAM fold to the jelly-roll family and reveals extensive interactions between the two domains, which form a rigid structural unit. Structure-based site-directed mutagenesis, serial domain deletions and cell-adhesion assays allowed us to identify the four N-terminal domains (MAM, Ig, fibronectin type III (FNIII)-1 and FNIII-2) as a minimal functional unit. Biophysical characterization revealed at least two independent types of homophilic interaction which, taken together, suggest that there is the potential for formation of a complex and possibly ordered array of receptor molecules at cell contact sites.

PubMed: 16456543
DOI: 10.1038/SJ.EMBOJ.7600974

Experimental method

X-RAY DIFFRACTION (2.7 Å)