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. 2003 Nov 28;302(5650):1571-5.
doi: 10.1126/science.1088372.

The structure of importin-beta bound to SREBP-2: nuclear import of a transcription factor

Soo Jae Lee  1 , Toshihiro Sekimoto, Eiki Yamashita, Emi Nagoshi, Atsushi Nakagawa, Naoko Imamoto, Masato Yoshimura, Hiroaki Sakai, Khoon Tee Chong, Tomitake Tsukihara, Yoshihiro Yoneda
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The structure of importin-beta bound to SREBP-2: nuclear import of a transcription factor

Soo Jae Lee et al. Science. .

Abstract

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-beta. We show the crystal structure of importin-beta complexed with the active form of SREBP-2. Importin-beta uses characteristic long helices like a pair of chopsticks to interact with an SREBP-2 dimer. Importin-beta changes its conformation to reveal a pseudo-twofold symmetry on its surface structure so that it can accommodate a symmetric dimer molecule. Importin-beta may use a similar strategy to recognize other dimeric cargoes.

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