1ial: Difference between revisions

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[[Image:1ial.gif|left|200px]]
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[[Image:1ial.png|left|200px]]


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{{STRUCTURE_1ial|  PDB=1ial  |  SCENE=  }}  
{{STRUCTURE_1ial|  PDB=1ial  |  SCENE=  }}  


'''IMPORTIN ALPHA, MOUSE'''
===IMPORTIN ALPHA, MOUSE===




==Overview==
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Importin alpha is the nuclear import receptor that recognizes classical monopartite and bipartite nuclear localization signals (NLSs). The structure of mouse importin alpha has been determined at 2.5 A resolution. The structure shows a large C-terminal domain containing armadillo repeats, and a less structured N-terminal importin beta-binding domain containing an internal NLS bound to the NLS-binding site. The structure explains the regulatory switch between the cytoplasmic, high-affinity form, and the nuclear, low-affinity form for NLS binding of the nuclear import receptor predicted by the current models of nuclear import. Importin beta conceivably converts the low- to high-affinity form by binding to a site overlapping the autoinhibitory sequence. The structure also has implications for understanding NLS recognition, and the structures of armadillo and HEAT repeats.
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{{ABSTRACT_PUBMED_10201409}}


==About this Structure==
==About this Structure==
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[[Category: Nuclear import receptor]]
[[Category: Nuclear import receptor]]
[[Category: Nuclear localization signal]]
[[Category: Nuclear localization signal]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:46:31 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:40:24 2008''

Revision as of 10:40, 1 July 2008

File:1ial.png

Template:STRUCTURE 1ial

IMPORTIN ALPHA, MOUSEIMPORTIN ALPHA, MOUSE

Template:ABSTRACT PUBMED 10201409

About this StructureAbout this Structure

1IAL is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin alpha., Kobe B, Nat Struct Biol. 1999 Apr;6(4):388-97. PMID:10201409

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