The Structure of Importin-ß Bound to SREBP-2: Nuclear Import of a Transcription Factor

The sterol regulatory element–binding protein 2 (SREBP-2), a nuclear transcription factor that is essential for cholesterol metabolism, enters the nucleus through a direct interaction of its helix-loop-helix leucine zipper domain with importin-β. We show the crystal structure of importin-β complexed...

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Veröffentlicht in:Science (American Association for the Advancement of Science) 2003-11, Vol.302 (5650), p.1571-1575
Hauptverfasser: Lee, Soo Jae, Sekimoto, Toshihiro, Yamashita, Eiki, Nagoshi, Emi, Nakagawa, Atsushi, Imamoto, Naoko, Yoshimura, Masato, Sakai, Hiroaki, Chong, Khoon Tee, Tsukihara, Tomitake, Yoneda, Yoshihiro
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container_issue 5650
container_start_page 1571
container_title Science (American Association for the Advancement of Science)
container_volume 302
creator Lee, Soo Jae
Sekimoto, Toshihiro
Yamashita, Eiki
Nagoshi, Emi
Nakagawa, Atsushi
Imamoto, Naoko
Yoshimura, Masato
Sakai, Hiroaki
Chong, Khoon Tee
Tsukihara, Tomitake
Yoneda, Yoshihiro
description The sterol regulatory element–binding protein 2 (SREBP-2), a nuclear transcription factor that is essential for cholesterol metabolism, enters the nucleus through a direct interaction of its helix-loop-helix leucine zipper domain with importin-β. We show the crystal structure of importin-β complexed with the active form of SREBP-2. Importin-β uses characteristic long helices like a pair of chopsticks to interact with an SREBP-2 dimer. Importin-β changes its conformation to reveal a pseudo-twofold symmetry on its surface structure so that it can accommodate a symmetric dimer molecule. Importin-β may use a similar strategy to recognize other dimeric cargoes.
doi_str_mv 10.1126/science.1088372
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title The Structure of Importin-ß Bound to SREBP-2: Nuclear Import of a Transcription Factor
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