2DDU

Crystal structure of the third repeat domain of reelin

Summary for 2DDU

• Entry DOI: 10.2210/pdb2ddu/pdb
• Descriptor: reelin, CALCIUM ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: beta-jelly-roll, signaling protein
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 1
• Total formula weight: 43402.80

Authors

Nogi, T.,Yasui, N.,Takagi, J. (deposition date: 2006-02-03, release date: 2006-09-26, Last modification date: 2024-10-23)

Primary citation

Nogi, T.,Yasui, N.,Hattori, M.,Iwasaki, K.,Takagi, J.
Structure of a signaling-competent reelin fragment revealed by X-ray crystallography and electron tomography
Embo J., 25:3675-3683, 2006

PubMed Abstract: 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.

PubMed: 16858396
DOI: 10.1038/sj.emboj.7601240

Experimental method

X-RAY DIFFRACTION (2.05 Å)