2ddu | pdb_00002ddu
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Crystal structure of the third repeat domain of reelin
Overview
The large extracellular glycoprotein reelin directs neuronal migration, during brain development and plays a fundamental role in layer formation., It is composed of eight tandem repeats of an approximately 380-residue, unit, termed the reelin repeat, which has a central epidermal growth, factor (EGF) module flanked by two homologous subrepeats with no obvious, sequence similarity to proteins of known structure. The 2.05 A crystal, structure of the mouse reelin repeat 3 reveals that the subrepeat assumes, a beta-jelly-roll fold with unexpected structural similarity to, carbohydrate-binding domains. Despite the interruption by the EGF module, the two subdomains make direct contact, resulting in a compact overall, structure. Electron micrographs of a four-domain fragment encompassing, repeats 3-6, which is capable of inducing Disabled-1 phosphorylation in, neurons, show a rod-like shape. Furthermore, a three-dimensional molecular, envelope of the fragment obtained by single-particle tomography can be, fitted with four concatenated repeat 3 atomic structures, providing the, first glimpse of the structural unit for this important signaling, molecule.
About this Structure
2DDU is a Single protein structure of sequence from Mus musculus with CA, CL and MG as ligands. Full crystallographic information is available from OCA.
Reference
Structure of a signaling-competent reelin fragment revealed by X-ray crystallography and electron tomography., Nogi T, Yasui N, Hattori M, Iwasaki K, Takagi J, EMBO J. 2006 Aug 9;25(15):3675-83. Epub 2006 Jul 20. PMID:16858396
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