1gcj
From Proteopedia
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| - | [[Image:1gcj.gif|left|200px]] | + | [[Image:1gcj.gif|left|200px]] |
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| - | '''N-TERMINAL FRAGMENT OF IMPORTIN-BETA''' | + | {{Structure |
| + | |PDB= 1gcj |SIZE=350|CAPTION= <scene name='initialview01'>1gcj</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''N-TERMINAL FRAGMENT OF IMPORTIN-BETA''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GCJ is a [ | + | 1GCJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCJ OCA]. |
==Reference== | ==Reference== | ||
| - | The adoption of a twisted structure of importin-beta is essential for the protein-protein interaction required for nuclear transport., Lee SJ, Imamoto N, Sakai H, Nakagawa A, Kose S, Koike M, Yamamoto M, Kumasaka T, Yoneda Y, Tsukihara T, J Mol Biol. 2000 Sep 8;302(1):251-64. PMID:[http:// | + | The adoption of a twisted structure of importin-beta is essential for the protein-protein interaction required for nuclear transport., Lee SJ, Imamoto N, Sakai H, Nakagawa A, Kose S, Koike M, Yamamoto M, Kumasaka T, Yoneda Y, Tsukihara T, J Mol Biol. 2000 Sep 8;302(1):251-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10964573 10964573] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nuclear pore-targeting complex component]] | [[Category: nuclear pore-targeting complex component]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:21:19 2008'' |
Revision as of 09:21, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
N-TERMINAL FRAGMENT OF IMPORTIN-BETA
Overview
Importin-beta is a nuclear transport factor which mediates the nuclear import of various nuclear proteins. The N-terminal 1-449 residue fragment of mouse importin-beta (impbeta449) possesses the ability to bidirectionally translocate through the nuclear pore complex (NPC), and to bind RanGTP. The structure of the uncomplexed form of impbeta449 has been solved at a 2.6 A resolution by X-ray crystallography. It consists of ten copies of the tandemly arrayed HEAT repeat and exhibits conformational flexibility which is involved in protein-protein interaction for nuclear transport. The overall conformation of the HEAT repeats shows that a twisted motion produces a significantly varied superhelical architecture from the previously reported structure of RanGTP-bound importin-beta. These conformational changes appear to be the sum of small conformational changes throughout the polypeptide. Such a flexibility, which resides in the stacked HEAT repeats, is essential for interaction with RanGTP or with NPCs. Furthermore, it was found that impbeta449 has a structural similarity with another nuclear migrating protein, namely beta-catenin, which is composed of another type of helix-repeated structure of ARM repeat. Interestingly, the essential regions for NPC translocation for both importin-beta and beta-catenin are spatially well overlapped with one another. This strongly indicates the importance of helix stacking of the HEAT or ARM repeats for NPC-passage.
About this Structure
1GCJ is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The adoption of a twisted structure of importin-beta is essential for the protein-protein interaction required for nuclear transport., Lee SJ, Imamoto N, Sakai H, Nakagawa A, Kose S, Koike M, Yamamoto M, Kumasaka T, Yoneda Y, Tsukihara T, J Mol Biol. 2000 Sep 8;302(1):251-64. PMID:10964573
Page seeded by OCA on Thu Mar 20 11:21:19 2008
