4YPC

Trimeric crystal structure of vimentin coil1B fragment

4YPC の概要

• エントリーDOI: 10.2210/pdb4ypc/pdb
• 関連するPDBエントリー: 3SWK
• 分子名称: Vimentin (2 entities in total)
• 機能のキーワード: cytoskeleton, intermediate filament, vimentin, alpha-helical coiled-coil trimer, structural protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm : P08670
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9924.02

構造登録者

Chernyatina, A.A.,Strelkov, S.V. (登録日: 2015-03-12, 公開日: 2015-12-02, 最終更新日: 2024-01-10)

主引用文献

Chernyatina, A.A.,Hess, J.F.,Guzenko, D.,Voss, J.C.,Strelkov, S.V.
How to Study Intermediate Filaments in Atomic Detail.
Meth. Enzymol., 568:3-33, 2016

PubMed Abstract: Studies of the intermediate filament (IF) structure are a prerequisite of understanding their function. In addition, the structural information is indispensable if one wishes to gain a mechanistic view on the disease-related mutations in the IFs. Over the years, considerable progress has been made on the atomic structure of the elementary building block of all IFs, the coiled-coil dimer. Here, we discuss the approaches, methods and practices that have contributed to this advance. With abundant genetic information on hand, bioinformatics approaches give important insights into the dimer structure, including the head and tail regions poorly assessable experimentally. At the same time, the most important contribution has been provided by X-ray crystallography. Following the "divide-and-conquer" approach, many fragments from several IF proteins could be crystallized and resolved to atomic resolution. We will systematically cover the main procedures of these crystallographic studies, suggest ways to maximize their efficiency, and also discuss the possible pitfalls and limitations. In addition, electron paramagnetic resonance with site-directed spin labeling was another method providing a major impact toward the understanding of the IF structure. Upon placing the spin labels into specific positions within the full-length protein, one can evaluate the proximity of the labels and their mobility. This makes it possible to make conclusions about the dimer structure in the coiled-coil region and beyond, as well as to explore the dimer-dimer contacts.

PubMed: 26795465
DOI: 10.1016/bs.mie.2015.09.024

実験手法

X-RAY DIFFRACTION (1.44 Å)