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1ukl

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[[Image:1ukl.jpg|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ukl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ukl OCA], [http://www.ebi.ac.uk/pdbsum/1ukl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ukl RCSB]</span>
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'''Crystal structure of Importin-beta and SREBP-2 complex'''
'''Crystal structure of Importin-beta and SREBP-2 complex'''
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[[Category: Yoneda, Y.]]
[[Category: Yoneda, Y.]]
[[Category: Yoshimura, M.]]
[[Category: Yoshimura, M.]]
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[[Category: heat repeat]]
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[[Category: Heat repeat]]
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[[Category: helix-loop-helix leucine zipper]]
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[[Category: Helix-loop-helix leucine zipper]]
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[[Category: nuclear transport factor]]
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[[Category: Nuclear transport factor]]
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[[Category: transcription factor]]
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[[Category: Transcription factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:21:24 2008''
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Revision as of 08:21, 3 May 2008

Template:STRUCTURE 1ukl

Crystal structure of Importin-beta and SREBP-2 complex


Overview

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.

About this Structure

1UKL is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

Reference

The structure of importin-beta bound to SREBP-2: nuclear import of a transcription factor., Lee SJ, Sekimoto T, Yamashita E, Nagoshi E, Nakagawa A, Imamoto N, Yoshimura M, Sakai H, Chong KT, Tsukihara T, Yoneda Y, Science. 2003 Nov 28;302(5650):1571-5. PMID:14645851 Page seeded by OCA on Sat May 3 11:21:24 2008

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