Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 408, Issue 4, Pages 616-627Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2011.03.013
Keywords
cell adhesion; receptor protein tyrosine phosphatase; heparan sulfate proteoglycans; immunoglobulin-like domains; crystal structure
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Funding
- National Institute Of General Medical Sciences [R01GM088806]
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [W-31-109-Eng-38]
- U.S. Department of Energy
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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.
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