Publication Date:
2003-12-03
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-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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Soo Jae -- Sekimoto, Toshihiro -- Yamashita, Eiki -- Nagoshi, Emi -- Nakagawa, Atsushi -- Imamoto, Naoko -- Yoshimura, Masato -- Sakai, Hiroaki -- Chong, Khoon Tee -- Tsukihara, Tomitake -- Yoneda, Yoshihiro -- New York, N.Y. -- Science. 2003 Nov 28;302(5650):1571-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Protein Research, Graduate School of Frontier Biosciences, Osaka University, Yamadaoka 2-2, Suita, Osaka 565-0871, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14645851" target="_blank"〉PubMed〈/a〉
Keywords:
*Active Transport, Cell Nucleus
;
Amino Acid Motifs
;
Amino Acid Sequence
;
Animals
;
Binding Sites
;
Cell Nucleus/metabolism
;
Crystallography, X-Ray
;
DNA-Binding Proteins/*chemistry/*metabolism
;
Dimerization
;
Helix-Loop-Helix Motifs
;
Humans
;
Hydrophobic and Hydrophilic Interactions
;
Mice
;
Models, Molecular
;
Molecular Sequence Data
;
Nuclear Localization Signals
;
Nuclear Pore/metabolism
;
Protein Binding
;
*Protein Conformation
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Sterol Regulatory Element Binding Protein 2
;
Transcription Factors/*chemistry/*metabolism
;
beta Karyopherins/*chemistry/*metabolism
;
ran GTP-Binding Protein/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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