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2c9a
From Proteopedia
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==Overview== | ==Overview== | ||
| - | 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 .. | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2C9A is a | + | 2C9A 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 NAG and NA 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] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C9A OCA]. |
==Reference== | ==Reference== | ||
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[[Category: receptor]] | [[Category: receptor]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:25:47 2007'' |
Revision as of 12:20, 5 November 2007
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CRYSTAL STRUCTURE OF THE MAM-IG MODULE OF RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU
Overview
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.
About this Structure
2C9A is a Single protein structure of sequence from Homo sapiens with NAG and NA as ligands. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion., Aricescu AR, Hon WC, Siebold C, Lu W, van der Merwe PA, Jones EY, EMBO J. 2006 Feb 22;25(4):701-12. Epub 2006 Feb 2. PMID:16456543
Page seeded by OCA on Mon Nov 5 14:25:47 2007
