Detail Structure of a Tyrosine Phosphatase Adhesive Interaction Reveals a Spacer-Clamp Mechanism   Oleh:  Aricescu, A. Radu ; Siebold, Christian ; Choudhuri, Kaushik ; Chang, Veronica T. ; Weixian, Lu ; Davis, Simon J. ; Merwe, P. Anton van der ; Jones, E. Yvonne Jenis: Article from Bulletin/Magazine Dalam koleksi: SCIENCE (keterangan: ada di Proquest) vol. 317 no. 5842 (Aug. 2007), page 1217. Ketersediaan Perpustakaan FK Nomor Panggil: S01.K.2007.07 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada     Lihat Detail Induk Isi artikel Cell-cell contacts are fundamental to multicellular organisms and are subject to exquisite levels of control. Human RPTPµ 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 RPTPµ 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 RPTPµ ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location. Opini Anda Klik untuk menuliskan opini Anda tentang koleksi ini! Kembali

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