|3pxj, resolution 2.30Å ()|
|Gene:||Lar, CG10443 (Drosophila melanogaster)|
Tandem Ig repeats of Dlar
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.
The Immunoglobulin-like Domains 1 and 2 of the Protein Tyrosine Phosphatase LAR Adopt an Unusual Horseshoe-like Conformation., Biersmith BH, Hammel M, Geisbrecht ER, Bouyain S, J Mol Biol. 2011 May 13;408(4):616-27. Epub 2011 Mar 21. PMID:21402080
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Biersmith BH, Hammel M, Geisbrecht ER, Bouyain S. The Immunoglobulin-like Domains 1 and 2 of the Protein Tyrosine Phosphatase LAR Adopt an Unusual Horseshoe-like Conformation. J Mol Biol. 2011 May 13;408(4):616-27. Epub 2011 Mar 21. PMID:21402080 doi:10.1016/j.jmb.2011.03.013
- ↑ Streuli M, Krueger NX, Tsai AY, Saito H. A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila. Proc Natl Acad Sci U S A. 1989 Nov;86(22):8698-702. PMID:2554325
- ↑ Krueger NX, Van Vactor D, Wan HI, Gelbart WM, Goodman CS, Saito H. The transmembrane tyrosine phosphatase DLAR controls motor axon guidance in Drosophila. Cell. 1996 Feb 23;84(4):611-22. PMID:8598047