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The immunoglobulin-like domains 1 and 2 of the protein tyrosine phosphatase LAR adopt an unusual horseshoe-like conformation.
- Source :
-
Journal of molecular biology [J Mol Biol] 2011 May 13; Vol. 408 (4), pp. 616-27. Date of Electronic Publication: 2011 Mar 21. - Publication Year :
- 2011
-
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.<br /> (Copyright © 2011 Elsevier Ltd. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Animals
Crystallography, X-Ray
Mice
Molecular Sequence Data
Nerve Tissue Proteins chemistry
Protein Structure, Secondary
Protein Structure, Tertiary
Drosophila Proteins chemistry
Immunoglobulins chemistry
Receptor-Like Protein Tyrosine Phosphatases chemistry
Receptor-Like Protein Tyrosine Phosphatases, Class 2 chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1089-8638
- Volume :
- 408
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Journal of molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 21402080
- Full Text :
- https://doi.org/10.1016/j.jmb.2011.03.013