2qmr
From Proteopedia
(New page: 200px<br /> <applet load="2qmr" size="450" color="white" frame="true" align="right" spinBox="true" caption="2qmr, resolution 3.00Å" /> '''Karyopherin beta2/t...) |
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| - | [[Image:2qmr.gif|left|200px]]<br /> | + | [[Image:2qmr.gif|left|200px]]<br /><applet load="2qmr" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2qmr" size=" | + | |
caption="2qmr, resolution 3.00Å" /> | caption="2qmr, resolution 3.00Å" /> | ||
'''Karyopherin beta2/transportin'''<br /> | '''Karyopherin beta2/transportin'''<br /> | ||
| - | == | + | ==Overview== |
| - | + | Karyopherinbeta2 (Kap beta2) or transportin imports numerous RNA binding, proteins into the nucleus. Kap beta2 binds substrates in the cytoplasm and, targets them through the nuclear pore complex, where RanGTP dissociates, them in the nucleus. Here we report the 3.0 A crystal structure of, unliganded Kap beta2, which consists of a superhelix of 20 HEAT repeats., Together with previously reported structures of NLS and Ran complexes, this structure provides understanding of conformational heterogeneity that, accompanies ligand binding. The Kap beta2 superhelix is divided into three, major segments. Two of them (HEAT repeats 9-13 and 14-18), which, constitute the substrate binding site, are rigid elements that rotate, relative to each other about a flexible hinge. The third (HEAT repeats, 1-8), which constitutes the Ran binding site, exhibits conformational, changes throughout its length. An analogous segmental architecture is also, observed in Importin beta, suggesting that it is functionally significant, and may be conserved in other import karyopherins. | |
==About this Structure== | ==About this Structure== | ||
| - | 2QMR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2QMR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QMR OCA]. |
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| + | ==Reference== | ||
| + | Conformational heterogeneity of karyopherin beta2 is segmental., Cansizoglu AE, Chook YM, Structure. 2007 Nov;15(11):1431-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17997969 17997969] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:03:04 2008'' |
Revision as of 09:03, 23 January 2008
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Karyopherin beta2/transportin
Overview
Karyopherinbeta2 (Kap beta2) or transportin imports numerous RNA binding, proteins into the nucleus. Kap beta2 binds substrates in the cytoplasm and, targets them through the nuclear pore complex, where RanGTP dissociates, them in the nucleus. Here we report the 3.0 A crystal structure of, unliganded Kap beta2, which consists of a superhelix of 20 HEAT repeats., Together with previously reported structures of NLS and Ran complexes, this structure provides understanding of conformational heterogeneity that, accompanies ligand binding. The Kap beta2 superhelix is divided into three, major segments. Two of them (HEAT repeats 9-13 and 14-18), which, constitute the substrate binding site, are rigid elements that rotate, relative to each other about a flexible hinge. The third (HEAT repeats, 1-8), which constitutes the Ran binding site, exhibits conformational, changes throughout its length. An analogous segmental architecture is also, observed in Importin beta, suggesting that it is functionally significant, and may be conserved in other import karyopherins.
About this Structure
2QMR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Conformational heterogeneity of karyopherin beta2 is segmental., Cansizoglu AE, Chook YM, Structure. 2007 Nov;15(11):1431-41. PMID:17997969
Page seeded by OCA on Wed Jan 23 11:03:04 2008
