The Immunoglobulin-like Domains 1 and 2 of the Protein Tyrosine Phosphatase LAR Adopt an Unusual Horseshoe-like Conformation

JOURNAL OF MOLECULAR BIOLOGY

卷:408

Article

Biersmith, Bridget H.²  Hammel, Michal³  Geisbrecht, Erika R.²  Bouyain, Samuel¹ 

[1] Univ Missouri, Sch Biol Sci, Div Mol Biol & Biochem, Kansas City, MO 64110 USA

[2] Univ Missouri, Sch Biol Sci, Div Cell Biol & Biophys, Kansas City, MO 64110 USA

[3] Univ Calif Berkeley, Lawrence Berkeley Lab, Phys Biosci Div, Berkeley, CA 94720 USA

关键词: cell adhesion;    receptor protein tyrosine phosphatase;    heparan sulfate proteoglycans;    immunoglobulin-like domains;    crystal structure;   

DOI  :  10.1016/j.jmb.2011.03.013

来源: Elsevier

【 摘 要 】

Neurogenesis depends on exquisitely regulated interactions between macromolecules on the cell surface and in the extracellular matrix. In particular, interactions between proteoglycans and members of the type Ha subgroup of receptor protein tyrosine phosphatases underlie crucial developmental processes such as the formation of synapses at the neuromuscular junction and the migration of axons to their appropriate targets. We report the crystal structures of the first and second immunoglobulin-like domains of the Drosophila type Ha receptor Dlar and its mouse homolog LAR. These two domains adopt an unusual antiparallel arrangement that has not been reported in tandem repeats of immunoglobulin-like domains and that is presumably conserved in all type Ha receptor protein tyrosine phosphatases. (C) 2011 Elsevier Ltd. All rights reserved.

【 授权许可】

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