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

被引:16
作者
Biersmith, Bridget H. [2 ]
Hammel, Michal [3 ]
Geisbrecht, Erika R. [2 ]
Bouyain, Samuel [1 ]
机构
[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; LIGAND-BINDING MODULE; MOTOR AXON GUIDANCE; CRYSTAL-STRUCTURE; MICE LACKING; SULFATE PROTEOGLYCAN; STRUCTURAL BASIS; RECEPTOR; HEPARIN; SHAPE; COMPUTATION;
D O I
10.1016/j.jmb.2011.03.013
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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.
引用
收藏
页码:616 / 627
页数:12
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