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 |
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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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