Identification of the homophilic binding site of the receptor protein tyrosine phosphatase PTP mu.

作者: S M Brady-Kalnay , N K Tonks

DOI: 10.1016/S0021-9258(18)46951-7

关键词: Binding siteFibronectinProtein tyrosine phosphataseBiologyTransmembrane proteinIntracellularTransmembrane domainImmunoglobulin domainMolecular biologyExtracellular

摘要: The receptor-type protein tyrosine phosphatase PTP mu comprises an extracellular segment containing a MAM domain, immunoglobulin domain and four fibronectin type III repeats, transmembrane segment, two intracellular domains. We have previously shown that binds homophilically, i.e. on the surface of one cell to apposing cell, alone is sufficient for homophilic binding. In this study we report in MvLu cells proteolytically processed into noncovalently associated fragments, comprising most (approximately 100 kDa) other predominantly portions kDa). also identified binding site within segment. generated, expressed, purified various fragments used fluorescent beads (Covaspheres) coated with these three assays: (i) measurement bead aggregation, (ii) surfaces dishes mu, or (iii) cells. Only recombinant contained underwent aggregation bound displaying suggesting neither nor repeats homophilically assays. fragment Ig as well any domain-containing fragment, both necessary under conditions.

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