2e26
From Proteopedia
Contents |
Crystal structure of two repeat fragment of reelin
Template:ABSTRACT PUBMED 17548821
Disease
[RELN_MOUSE] Note=Defects in Reln are the cause of the autosomal recessive reeler (rl) phenotype which is characterized by impaired motor coordination, tremors and ataxia. Neurons in affected mice fail to reach their correct locations in the developing brain, disrupting the organization of the cerebellar and cerebral cortices and other laminated regions.
Function
[RELN_MOUSE] Extracellular matrix serine protease that plays a role in layering of neurons in the cerebral cortex and cerebellum. Regulates microtubule function in neurons and neuronal migration. Affects migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migration. Enzymatic activity is important for the modulation of cell adhesion. Binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of TAU phosphorylation.[1]
About this Structure
2e26 is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
- Yasui N, Nogi T, Kitao T, Nakano Y, Hattori M, Takagi J. Structure of a receptor-binding fragment of reelin and mutational analysis reveal a recognition mechanism similar to endocytic receptors. Proc Natl Acad Sci U S A. 2007 Jun 12;104(24):9988-93. Epub 2007 Jun 4. PMID:17548821
- ↑ Yip JW, Yip YP, Nakajima K, Capriotti C. Reelin controls position of autonomic neurons in the spinal cord. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8612-6. PMID:10880573 doi:10.1073/pnas.150040497
