2ddu

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(New page: 200px<br /><applet load="2ddu" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ddu, resolution 2.05&Aring;" /> '''Crystal structure of...)
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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: beta-jelly-roll]]
[[Category: beta-jelly-roll]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:01:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:57:47 2008''

Revision as of 14:57, 21 February 2008

Image:2ddu.gif

2ddu, resolution 2.05Å

Drag the structure with the mouse to rotate

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 , and 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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