1jn5

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spinqualitylabelsall models 1jn5, resolution 2.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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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