Abstract:
: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 IIa 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 IIa 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 IIa receptor protein tyrosine phosphatases.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Biersmith BH,Hammel M,Geisbrecht ER,Bouyain Sdoi
10.1016/j.jmb.2011.03.013subject
Has Abstractpub_date
2011-05-13 00:00:00pages
616-27issue
4eissn
0022-2836issn
1089-8638pii
S0022-2836(11)00278-6journal_volume
408pub_type
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