1jn5
From Proteopedia
(New page: 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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caption="1jn5, resolution 2.8Å" /> | caption="1jn5, resolution 2.8Å" /> | ||
'''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:// | + | 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:// | + | ''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
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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
Contents |
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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