3ND2

Structure of Yeast Importin-beta (Kap95p)

3ND2 の概要

• エントリーDOI: 10.2210/pdb3nd2/pdb
• 分子名称: Importin subunit beta-1 (2 entities in total)
• 機能のキーワード: importin, karyopherin, nuclear import, receptor, nuclear transport, transport protein
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• 細胞内の位置: Cytoplasm (By similarity): Q06142
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 94843.27

構造登録者

Forwood, J.K.,Kobe, B. (登録日: 2010-06-06, 公開日: 2010-07-07, 最終更新日: 2023-11-01)

主引用文献

Forwood, J.K.,Lange, A.,Zachariae, U.,Marfori, M.,Preast, C.,Grubmuller, H.,Stewart, M.,Corbett, A.H.,Kobe, B.
Quantitative Structural Analysis of Importin-beta Flexibility: Paradigm for Solenoid Protein Structures
Structure, 18:1171-1183, 2010

PubMed Abstract: The structure of solenoid proteins facilitates a higher degree of flexibility than most folded proteins. In importin-β, a nuclear import factor built from 19 tandem HEAT repeats, flexibility plays a crucial role in allowing interactions with a range of different partners. We present a comprehensive analysis of importin-β flexibility based on a number of different approaches. We determined the crystal structure of unliganded Saccharomyces cerevisiae importin-β (Kap95) to allow a quantitative comparison with importin-β bound to different partners. Complementary mutagenesis, small angle X-ray scattering and molecular dynamics studies suggest that the protein samples several conformations in solution. The analyses suggest the flexibility of the solenoid is generated by cumulative small movements along its length. Importin-β illustrates how solenoid proteins can orchestrate protein interactions in many cellular pathways.

PubMed: 20826343
DOI: 10.1016/j.str.2010.06.015

実験手法

X-RAY DIFFRACTION (2.4 Å)