1jn5: Difference between revisions

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New page: left|200px<br /> <applet load="1jn5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jn5, resolution 2.8Å" /> '''Structural basis for...
 
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[[Image:1jn5.gif|left|200px]]<br />
[[Image:1jn5.jpg|left|200px]]<br /><applet load="1jn5" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1jn5" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1jn5, resolution 2.8&Aring;" />
caption="1jn5, resolution 2.8&Aring;" />
'''Structural basis for the recognition of a nucleoporin FG-repeat by the NTF2-like domain of TAP-p15 mRNA export factor'''<br />
'''Structural basis for the recognition of a nucleoporin FG-repeat by the NTF2-like domain of TAP-p15 mRNA export factor'''<br />
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==About this Structure==
==About this Structure==
1JN5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JN5 OCA].  
1JN5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1JN5 OCA].  


==Reference==
==Reference==
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[[Category: nucleoporin]]
[[Category: nucleoporin]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:42:43 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:08:09 2008''

Revision as of 14:08, 15 February 2008

File:1jn5.jpg


1jn5, resolution 2.8Å

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Structural basis for the recognition of a nucleoporin FG-repeat by the NTF2-like domain of TAP-p15 mRNA export factor

Overview

TAP-p15 heterodimers have been implicated in the export of mRNAs through, nuclear pore complexes (NPCs). We report a structural analysis of the, interaction domains of TAP and p15 in a ternary complex with a Phe-Gly, (FG) repeat of an NPC component. The TAP-p15 heterodimer is structurally, similar to the homodimeric transport factor NTF2, but unlike NTF2, it is, incompatible with either homodimerization or Ran binding. The NTF2-like, heterodimer functions as a single structural unit in recognizing an FG, repeat at a hydrophobic pocket present only on TAP and not on p15. This FG, binding site interacts synergistically with a second site at the C, terminus of TAP to mediate mRNA transport through the pore. In general, our findings suggest that FG repeats bind with a similar conformation to, different classes of transport factors.

Disease

Known diseases associated with this structure: Bare lymphocyte syndrome, type I OMIM:[170260]

About this Structure

1JN5 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor., Fribourg S, Braun IC, Izaurralde E, Conti E, Mol Cell. 2001 Sep;8(3):645-56. PMID:11583626

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