1qgk

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(New page: 200px<br /> <applet load="1qgk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qgk, resolution 2.5&Aring;" /> '''STRUCTURE OF IMPORTI...)
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<applet load="1qgk" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1qgk, resolution 2.5&Aring;" />
'''STRUCTURE OF IMPORTIN BETA BOUND TO THE IBB DOMAIN OF IMPORTIN ALPHA'''<br />
'''STRUCTURE OF IMPORTIN BETA BOUND TO THE IBB DOMAIN OF IMPORTIN ALPHA'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1QGK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1QGK with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb85_1.html Importins]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QGK OCA].
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1QGK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1QGK with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb85_1.html Importins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QGK OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Cingolani, G.]]
[[Category: Cingolani, G.]]
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[[Category: Muller, C.W.]]
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[[Category: Muller, C W.]]
[[Category: Petosa, C.]]
[[Category: Petosa, C.]]
[[Category: Weis, K.]]
[[Category: Weis, K.]]
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[[Category: transport receptor]]
[[Category: transport receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:52:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:17 2008''

Revision as of 12:39, 21 February 2008


1qgk, resolution 2.5Å

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STRUCTURE OF IMPORTIN BETA BOUND TO THE IBB DOMAIN OF IMPORTIN ALPHA

Overview

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.

About this Structure

1QGK is a Protein complex structure of sequences from Homo sapiens. The following page contains interesting information on the relation of 1QGK with [Importins]. Full crystallographic information is available from OCA.

Reference

Structure of importin-beta bound to the IBB domain of importin-alpha., Cingolani G, Petosa C, Weis K, Muller CW, Nature. 1999 May 20;399(6733):221-9. PMID:10353244

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