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Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1.

Nature structural biology | Apr 26, 2002

The vertebrate Tap protein is a member of the NXF family of shuttling transport receptors for nuclear export of mRNA. Tap has a modular structure, and its most C-terminal domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate nuclear shuttling. We report the solution structure of this C-terminal domain, which is based on a distinctive arrangement of four alpha-helices and is joined to the next module by a flexible 12-residue Pro-rich linker. F617A Tap suppresses FG-nucleoporin binding by the most C-terminal domain that, together with the structure of the other modules from which Tap is constructed, provides a structural context for its nuclear shuttling function.

Pubmed ID: 11875519 RIS Download

Mesh terms: Amino Acid Sequence | Animals | Binding Sites | Circular Dichroism | Humans | Hydrophobic and Hydrophilic Interactions | Models, Molecular | Molecular Sequence Data | Nuclear Magnetic Resonance, Biomolecular | Nuclear Pore Complex Proteins | Nuclear Proteins | Nucleocytoplasmic Transport Proteins | Protein Binding | Protein Structure, Tertiary | RNA-Binding Proteins | Repetitive Sequences, Amino Acid | Sequence Alignment | Structure-Activity Relationship