1jkg

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(New page: 200px<br /> <applet load="1jkg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jkg, resolution 1.9&Aring;" /> '''Structural basis for...)
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'''Structural basis for the recognition of a nucleoporin FG-repeat by the NTF2-like domain of TAP-p15 mRNA nuclear export factor'''<br />
'''Structural basis for the recognition of a nucleoporin FG-repeat by the NTF2-like domain of TAP-p15 mRNA nuclear export factor'''<br />
==Overview==
==Overview==
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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.
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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==
==Disease==
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==About this Structure==
==About this Structure==
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1JKG 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=1JKG OCA].
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1JKG 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=1JKG OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Braun, I.C.]]
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[[Category: Braun, I C.]]
[[Category: Conti, E.]]
[[Category: Conti, E.]]
[[Category: Fribourg, S.]]
[[Category: Fribourg, S.]]
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[[Category: ntf2-like domain]]
[[Category: ntf2-like domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:41:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:39 2008''

Revision as of 11:23, 21 February 2008


1jkg, resolution 1.9Å

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

1JKG 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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