3GB8

Crystal structure of CRM1/Snurportin-1 complex

Summary for 3GB8

• Entry DOI: 10.2210/pdb3gb8/pdb
• Descriptor: Exportin-1, Snurportin-1 (2 entities in total)
• Functional Keywords: nuclear transport complex, host-virus interaction, mrna transport, nucleus, phosphoprotein, protein transport, rna-binding, transport, transport protein
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm: O14980; Nucleus : O95149
• Total number of polymer chains: 2
• Total formula weight: 161285.12

Authors

Dong, X.,Biswas, A.,Suel, K.E.,Jackson, L.K.,Martinez, R.,Gu, H.,Chook, Y.M. (deposition date: 2009-02-19, release date: 2009-03-31, Last modification date: 2024-02-21)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.9 Å)