6HYF

Crystal structure of the third FNIII domain from rat beta4 integrin, a binding site for periaxin

6HYF の概要

• エントリーDOI: 10.2210/pdb6hyf/pdb
• 分子名称: Integrin beta-4 (2 entities in total)
• 機能のキーワード: myelin, integrin, periaxin, protein binding
• 由来する生物種: Rattus norvegicus (Norway rat)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 51100.82

構造登録者

Raasakka, A.,Kursula, P. (登録日: 2018-10-20, 公開日: 2019-05-08, 最終更新日: 2024-01-24)

主引用文献

Raasakka, A.,Linxweiler, H.,Brophy, P.J.,Sherman, D.L.,Kursula, P.
Direct Binding of the Flexible C-Terminal Segment of Periaxin to beta 4 Integrin Suggests a Molecular Basis for CMT4F.
Front Mol Neurosci, 12:84-84, 2019

PubMed Abstract: The process of myelination in the nervous system requires a coordinated formation of both transient and stable supramolecular complexes. Myelin-specific proteins play key roles in these assemblies, which may link membranes to each other or connect the myelinating cell cytoskeleton to the extracellular matrix. The myelin protein periaxin is known to play an important role in linking the Schwann cell cytoskeleton to the basal lamina through membrane receptors, such as the dystroglycan complex. Mutations that truncate periaxin from the C terminus cause demyelinating peripheral neuropathy, Charcot-Marie-Tooth (CMT) disease type 4F, indicating a function for the periaxin C-terminal region in myelination. We identified the cytoplasmic domain of β4 integrin as a specific high-affinity binding partner for periaxin. The C-terminal region of periaxin remains unfolded and flexible when bound to the third fibronectin type III domain of β4 integrin. Our data suggest that periaxin is able to link the Schwann cell cytoplasm to the basal lamina through a two-pronged interaction different membrane protein complexes, which bind close to the N and C terminus of this elongated, flexible molecule.

PubMed: 31024253
DOI: 10.3389/fnmol.2019.00084

実験手法

X-RAY DIFFRACTION (1.6 Å)