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1UKL

Crystal structure of Importin-beta and SREBP-2 complex

Summary for 1UKL
Entry DOI10.2210/pdb1ukl/pdb
DescriptorImportin beta-1 subunit, Sterol regulatory element binding protein-2 (2 entities in total)
Functional Keywordstranscription factor, nuclear transport factor, heat repeat, helix-loop-helix leucine zipper, protein transport-dna binding protein complex, protein transport/dna binding protein
Biological sourceMus musculus (house mouse)
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Cellular locationCytoplasm (By similarity): P70168
Endoplasmic reticulum membrane; Multi-pass membrane protein. Processed sterol regulatory element-binding protein 2: Nucleus: Q12772
Total number of polymer chains6
Total formula weight223652.20
Authors
Lee, S.J.,Sekimoto, T.,Yamashita, E.,Nagoshi, E.,Nakagawa, A.,Imamoto, N.,Yoshimura, M.,Sakai, H.,Tsukihara, T.,Yoneda, Y. (deposition date: 2003-08-26, release date: 2003-12-09, Last modification date: 2024-10-23)
Primary citationLee, S.J.,Sekimoto, T.,Yamashita, E.,Nagoshi, E.,Nakagawa, A.,Imamoto, N.,Yoshimura, M.,Sakai, H.,Chong, K.T.,Tsukihara, T.,Yoneda, Y.
The Structure of Importin-beta Bound to SREBP-2: Nuclear Import of a Transcription Factor
Science, 302:1571-1575, 2003
Cited by
PubMed 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.
PubMed: 14645851
DOI: 10.1126/science.1088372
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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