6BVV

Nipah virus W protein C-terminus in complex with Importin alpha 3

6BVV の概要

• エントリーDOI: 10.2210/pdb6bvv/pdb
• 関連するPDBエントリー: 6BVT
• 分子名称: Importin subunit alpha-3, Protein W (3 entities in total)
• 機能のキーワード: complex, nipah virus, importin, karyopherin, phosphoprotein, w, transport protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55099.50

構造登録者

Smith, K.M.,Tsimbalyuk, S.,Edwards, M.R.,Aragao, D.,Cross, E.M.,Basler, C.F.,Forwood, J.K. (登録日: 2017-12-13, 公開日: 2018-07-04, 最終更新日: 2024-05-22)

主引用文献

Smith, K.M.,Tsimbalyuk, S.,Edwards, M.R.,Cross, E.M.,Batra, J.,Soares da Costa, T.P.,Aragao, D.,Basler, C.F.,Forwood, J.K.
Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses.
Nat Commun, 9:3703-3703, 2018

PubMed Abstract: Seven human isoforms of importin α mediate nuclear import of cargo in a tissue- and isoform-specific manner. How nuclear import adaptors differentially interact with cargo harbouring the same nuclear localisation signal (NLS) remains poorly understood, as the NLS recognition region is highly conserved. Here, we provide a structural basis for the nuclear import specificity of W proteins in Hendra and Nipah viruses. We determine the structural interfaces of these cargo bound to importin α1 and α3, identifying a 2.4-fold more extensive interface and > 50-fold higher binding affinity for importin α3. Through the design of importin α1 and α3 chimeric and mutant proteins, together with structures of cargo-free importin α1 and α3 isoforms, we establish that the molecular basis of specificity resides in the differential positioning of the armadillo repeats 7 and 8. Overall, our study provides mechanistic insights into a range of important nucleocytoplasmic transport processes reliant on isoform adaptor specificity.

PubMed: 30209309
DOI: 10.1038/s41467-018-05928-5

実験手法

X-RAY DIFFRACTION (2.3 Å)