2ddu
From Proteopedia
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'''Crystal structure of the third repeat domain of reelin''' | '''Crystal structure of the third repeat domain of reelin''' | ||
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[[Category: Takagi, J.]] | [[Category: Takagi, J.]] | ||
[[Category: Yasui, N.]] | [[Category: Yasui, N.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:14:28 2008'' | |
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Revision as of 21:14, 3 May 2008
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. 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 Page seeded by OCA on Sun May 4 00:14:28 2008
