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

Autor: Masato Yoshimura, Tomitake Tsukihara, Hiroaki Sakai, Eiki Yamashita, Soo Jae Lee, Atsushi Nakagawa, Yoshihiro Yoneda, Emi Nagoshi, Naoko Imamoto, Khoon Tee Chong, Toshihiro Sekimoto
Rok vydání: 2003
Předmět:
Models
Molecular
Leucine zipper
animal structures
Protein Conformation
Amino Acid Motifs
Molecular Sequence Data
Nuclear Localization Signals
Active Transport
Cell Nucleus
Importin
Biology
Crystallography
X-Ray
environment and public health
Protein Structure
Secondary
Mice
Protein structure
Animals
Humans
Amino Acid Sequence
Binding site
Transcription factor
Cell Nucleus
Binding Sites
Multidisciplinary
Helix-Loop-Helix Motifs
beta Karyopherins
Protein Structure
Tertiary
Sterol regulatory element-binding protein
DNA-Binding Proteins
ran GTP-Binding Protein
Biochemistry
embryonic structures
Nuclear Pore
Biophysics
lipids (amino acids
peptides
and proteins)
Sterol regulatory element-binding protein 2
Nuclear transport
Dimerization
Hydrophobic and Hydrophilic Interactions
Protein Binding
Sterol Regulatory Element Binding Protein 2
Transcription Factors
Zdroj: Science. 302:1571-1575
ISSN: 1095-9203
0036-8075
DOI: 10.1126/science.1088372
Popis: 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.
Databáze: OpenAIRE
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