3GB8

Crystal structure of CRM1/Snurportin-1 complex

3GB8 の概要

• エントリーDOI: 10.2210/pdb3gb8/pdb
• 分子名称: Exportin-1, Snurportin-1 (2 entities in total)
• 機能のキーワード: nuclear transport complex, host-virus interaction, mrna transport, nucleus, phosphoprotein, protein transport, rna-binding, transport, transport protein
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Cytoplasm: O14980; Nucleus : O95149
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 161285.12

構造登録者

Dong, X.,Biswas, A.,Suel, K.E.,Jackson, L.K.,Martinez, R.,Gu, H.,Chook, Y.M. (登録日: 2009-02-19, 公開日: 2009-03-31, 最終更新日: 2024-02-21)

主引用文献

Dong, X.,Biswas, A.,Suel, K.E.,Jackson, L.K.,Martinez, R.,Gu, H.,Chook, Y.M.
Structural basis for leucine-rich nuclear export signal recognition by CRM1.
Nature, 458:1136-1141, 2009

PubMed Abstract: CRM1 (also known as XPO1 and exportin 1) mediates nuclear export of hundreds of proteins through the recognition of the leucine-rich nuclear export signal (LR-NES). Here we present the 2.9 A structure of CRM1 bound to snurportin 1 (SNUPN). Snurportin 1 binds CRM1 in a bipartite manner by means of an amino-terminal LR-NES and its nucleotide-binding domain. The LR-NES is a combined alpha-helical-extended structure that occupies a hydrophobic groove between two CRM1 outer helices. The LR-NES interface explains the consensus hydrophobic pattern, preference for intervening electronegative residues and inhibition by leptomycin B. The second nuclear export signal epitope is a basic surface on the snurportin 1 nucleotide-binding domain, which binds an acidic patch on CRM1 adjacent to the LR-NES site. Multipartite recognition of individually weak nuclear export signal epitopes may be common to CRM1 substrates, enhancing CRM1 binding beyond the generally low affinity LR-NES. Similar energetic construction is also used in multipartite nuclear localization signals to provide broad substrate specificity and rapid evolution in nuclear transport.

PubMed: 19339969
DOI: 10.1038/nature07975

実験手法

X-RAY DIFFRACTION (2.9 Å)