1bk5: Difference between revisions

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New page: left|200px<br /><applet load="1bk5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bk5, resolution 2.2Å" /> '''KARYOPHERIN ALPHA FRO...
 
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[[Image:1bk5.gif|left|200px]]<br /><applet load="1bk5" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1bk5.gif|left|200px]]<br /><applet load="1bk5" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1bk5, resolution 2.2&Aring;" />
caption="1bk5, resolution 2.2&Aring;" />
'''KARYOPHERIN ALPHA FROM SACCHAROMYCES CEREVISIAE'''<br />
'''KARYOPHERIN ALPHA FROM SACCHAROMYCES CEREVISIAE'''<br />


==Overview==
==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.
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==
1BK5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with CO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BK5 OCA].  
1BK5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=CO:'>CO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BK5 OCA].  


==Reference==
==Reference==
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[[Category: protein transport]]
[[Category: protein transport]]


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Revision as of 12:56, 21 February 2008

File:1bk5.gif


1bk5, resolution 2.2Å

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KARYOPHERIN ALPHA FROM SACCHAROMYCES CEREVISIAE

OverviewOverview

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 StructureAbout this Structure

1BK5 is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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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