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| {{STRUCTURE_2c9a| PDB=2c9a | SCENE= }} | | {{STRUCTURE_2c9a| PDB=2c9a | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF THE MAM-IG MODULE OF RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU'''
| | ===CRYSTAL STRUCTURE OF THE MAM-IG MODULE OF RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16456543}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16456543 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16456543}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Immunoglobulin domain]] | | [[Category: Immunoglobulin domain]] |
| [[Category: Receptor]] | | [[Category: Receptor]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:29:43 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:14:43 2008'' |
