1bk6

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(New page: 200px<br /><applet load="1bk6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bk6, resolution 2.8&Aring;" /> '''KARYOPHERIN ALPHA (YE...)
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[[Image:1bk6.gif|left|200px]]<br /><applet load="1bk6" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1bk6.gif|left|200px]]<br /><applet load="1bk6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1bk6, resolution 2.8&Aring;" />
caption="1bk6, resolution 2.8&Aring;" />
'''KARYOPHERIN ALPHA (YEAST) + SV40 T ANTIGEN NLS'''<br />
'''KARYOPHERIN ALPHA (YEAST) + SV40 T ANTIGEN NLS'''<br />
==Overview==
==Overview==
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Selective nuclear import is mediated by nuclear localization signals, (NLSs) and cognate transport factors known as karyopherins or importins., Karyopherin alpha recognizes "classical" monopartite and bipartite NLSs., We report the crystal structure of a 50 kDa fragment of the 60 kDa yeast, karyopherin alpha, in the absence and presence of a monopartite NLS, peptide at 2.2 A and 2.8 A resolution, respectively. The structure shows a, tandem array of ten armadillo repeats, organized in a right-handed, superhelix of helices. Binding of the NLS peptide occurs at two sites, within a helical surface groove that is lined by conserved residues. The, structure reveals the determinants of NLS specificity and suggests a model, for the recognition of bipartite NLSs.
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Selective nuclear import is mediated by nuclear localization signals (NLSs) and cognate transport factors known as karyopherins or importins. Karyopherin alpha recognizes "classical" monopartite and bipartite NLSs. We report the crystal structure of a 50 kDa fragment of the 60 kDa yeast karyopherin alpha, in the absence and presence of a monopartite NLS peptide at 2.2 A and 2.8 A resolution, respectively. The structure shows a tandem array of ten armadillo repeats, organized in a right-handed superhelix of helices. Binding of the NLS peptide occurs at two sites within a helical surface groove that is lined by conserved residues. The structure reveals the determinants of NLS specificity and suggests a model for the recognition of bipartite NLSs.
==About this Structure==
==About this Structure==
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1BK6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BK6 OCA].
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1BK6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BK6 OCA].
==Reference==
==Reference==
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[[Category: protein transport]]
[[Category: protein transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:43:03 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:10 2008''

Revision as of 09:56, 21 February 2008


1bk6, resolution 2.8Å

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KARYOPHERIN ALPHA (YEAST) + SV40 T ANTIGEN NLS

Overview

Selective nuclear import is mediated by nuclear localization signals (NLSs) and cognate transport factors known as karyopherins or importins. Karyopherin alpha recognizes "classical" monopartite and bipartite NLSs. We report the crystal structure of a 50 kDa fragment of the 60 kDa yeast karyopherin alpha, in the absence and presence of a monopartite NLS peptide at 2.2 A and 2.8 A resolution, respectively. The structure shows a tandem array of ten armadillo repeats, organized in a right-handed superhelix of helices. Binding of the NLS peptide occurs at two sites within a helical surface groove that is lined by conserved residues. The structure reveals the determinants of NLS specificity and suggests a model for the recognition of bipartite NLSs.

About this Structure

1BK6 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha., Conti E, Uy M, Leighton L, Blobel G, Kuriyan J, Cell. 1998 Jul 24;94(2):193-204. PMID:9695948

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