5X8N

Crystal structure of mouse importin-alpha1 bound to the nuclear localization signal of Epstein-Barr virus EBNA-LP protein

Summary for 5X8N

• Entry DOI: 10.2210/pdb5x8n/pdb
• Descriptor: Importin subunit alpha-1, Epstein-Barr nuclear antigen leader protein (3 entities in total)
• Functional Keywords: importin, nls, ebna-lp, epstein-barr virus, protein transport-transcription complex, protein transport/transcription
• Biological source: Mus musculus (Mouse); More
• Cellular location: Cytoplasm : P52293; Host nucleus : Q8AZK7
• Total number of polymer chains: 2
• Total formula weight: 52593.75

Authors

Nakada, R.,Matsuura, Y. (deposition date: 2017-03-03, release date: 2017-04-19, Last modification date: 2023-11-22)

Primary citation

Nakada, R.,Matsuura, Y.
Crystal structure of importin-alpha bound to the nuclear localization signal of Epstein-Barr virus EBNA-LP protein
Protein Sci., 26:1231-1235, 2017

PubMed Abstract: Epstein-Barr virus EBNA-LP protein is a transcriptional coactivator of EBNA2. Efficient nuclear localization of EBNA-LP is essential for cooperation with EBNA2. Here, we report the crystal structure of the nuclear import adaptor importin-α1 bound to the nuclear localization signal (NLS) of EBNA-LP that shows EBNA-LP residues 44-RRVRRR-49 binding to the major NLS-binding site at the P0-P5 positions. In contrast to previously characterized classical NLSs that invariably have a basic residue [either lysine (in the vast majority of cases) or arginine] at the P2 position, the EBNA-LP NLS is unique in that it has valine at the P2 position. The loss of the critical P2 lysine (or arginine) is compensated by arginine at the P0 position in the EBNA-LP NLS.

PubMed: 28383161
DOI: 10.1002/pro.3173

Experimental method

X-RAY DIFFRACTION (2.15 Å)