1jn5
From Proteopedia
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==Overview== | ==Overview== | ||
| - | TAP-p15 heterodimers have been implicated in the export of mRNAs through | + | 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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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Braun, I | + | [[Category: Braun, I C.]] |
[[Category: Conti, E.]] | [[Category: Conti, E.]] | ||
[[Category: Fribourg, S.]] | [[Category: Fribourg, S.]] | ||
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[[Category: nucleoporin]] | [[Category: nucleoporin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:29 2008'' |
Revision as of 11:24, 21 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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