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| {{STRUCTURE_1qgr| PDB=1qgr | SCENE= }} | | {{STRUCTURE_1qgr| PDB=1qgr | SCENE= }} |
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| '''STRUCTURE OF IMPORTIN BETA BOUND TO THE IBB DOMAIN OF IMPORTIN ALPHA (II CRYSTAL FORM, GROWN AT LOW PH)'''
| | ===STRUCTURE OF IMPORTIN BETA BOUND TO THE IBB DOMAIN OF IMPORTIN ALPHA (II CRYSTAL FORM, GROWN AT LOW PH)=== |
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| ==Overview==
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| Cytosolic proteins bearing a classical nuclear localization signal enter the nucleus bound to a heterodimer of importin-alpha and importin-beta (also called karyopherin-alpha and -beta). The formation of this heterodimer involves the importin-beta-binding (IBB) domain of importin-alpha, a highly basic amino-terminal region of roughly 40 amino-acid residues. Here we report the crystal structure of human importin-beta bound to the IBB domain of importin-alpha, determined at 2.5 A and 2.3 A resolution in two crystal forms. Importin-beta consists of 19 tandemly repeated HEAT motifs and wraps intimately around the IBB domain. The association involves two separate regions of importin-beta, recognizing structurally distinct parts of the IBB domain: an amino-terminal extended moiety and a carboxy-terminal helix. The structure indicates that significant conformational changes occur when importin-beta binds or releases the IBB domain domain and suggests how dissociation of the importin-alpha/beta heterodimer may be achieved upon nuclear entry.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10353244}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10353244 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10353244}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Nuclear import]] | | [[Category: Nuclear import]] |
| [[Category: Transport receptor]] | | [[Category: Transport receptor]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:15:00 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:03:29 2008'' |
