2bku

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[[Image:2bku.gif|left|200px]]<br /><applet load="2bku" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bku.gif|left|200px]]<br /><applet load="2bku" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2bku, resolution 2.70&Aring;" />
caption="2bku, resolution 2.70&Aring;" />
'''KAP95P:RANGTP COMPLEX'''<br />
'''KAP95P:RANGTP COMPLEX'''<br />
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==About this Structure==
==About this Structure==
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2BKU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG and GTP as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 2BKU with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb85_1.html Importins]]. Known structural/functional Site: <scene name='pdbsite=AC1:Mg Binding Site For Chain C'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BKU OCA].
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2BKU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GTP:'>GTP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 2BKU with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb85_1.html Importins]]. Known structural/functional Site: <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+C'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BKU OCA].
==Reference==
==Reference==
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[[Category: rangtp]]
[[Category: rangtp]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:50:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:25:15 2008''

Revision as of 08:25, 3 February 2008


2bku, resolution 2.70Å

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KAP95P:RANGTP COMPLEX

Overview

Nuclear protein import is mediated mainly by the transport factor, importin-beta that binds cytoplasmic cargo, most often via the, importin-alpha adaptor, and then transports it through nuclear pore, complexes. This active transport is driven by disassembly of the import, complex by nuclear RanGTP. The switch I and II loops of Ran change, conformation with nucleotide state, and regulate its interactions with, nuclear trafficking components. Importin-beta consists of 19 HEAT repeats, that are based on a pair of antiparallel alpha-helices (referred to as the, A- and B-helices). The HEAT repeats stack to yield two C-shaped arches, linked together to form a helicoidal molecule that has considerable, conformational flexibility. Here we present the structure of full-length, yeast importin-beta (Kap95p or karyopherin-beta) complexed with RanGTP, which provides a basis for understanding the crucial cargo-release step of, nuclear import. We identify a key interaction site where the RanGTP switch, I loop binds to the carboxy-terminal arch of Kap95p. This interaction, produces a change in helicoidal pitch that locks Kap95p in a conformation, that cannot bind importin-alpha or cargo. We suggest an allosteric, mechanism for nuclear import complex disassembly by RanGTP.

About this Structure

2BKU is a Protein complex structure of sequences from Canis lupus familiaris and Saccharomyces cerevisiae with and as ligands. The following page contains interesting information on the relation of 2BKU with [Importins]. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structural basis for nuclear import complex dissociation by RanGTP., Lee SJ, Matsuura Y, Liu SM, Stewart M, Nature. 2005 Jun 2;435(7042):693-6. Epub 2005 May 1. PMID:15864302

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