1GO5

Structure of the C-terminal FG-binding domain of human Tap

Summary for 1GO5

• Entry DOI: 10.2210/pdb1go5/pdb
• Related: 1FO1
• NMR Information: BMRB: 5364
• Descriptor: TIP ASSOCIATING PROTEIN (1 entity in total)
• Functional Keywords: nuclear transport, mrna export, uba, nucleoporins
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 7718.60

Authors

Grant, R.P.,Hurt, E.,Neuhaus, D.,Stewart, M. (deposition date: 2001-10-18, release date: 2002-02-05, Last modification date: 2024-05-15)

Primary citation

Grant, R.P.,Hurt, E.,Neuhaus, D.,Stewart, M.
Structure of the C-Terminal Fg-Nucleoporin Binding Domain of Tap/Nxf1
Nat.Struct.Biol., 9:247-, 2002

PubMed Abstract: 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: 11875519
DOI: 10.1038/NSB773

Experimental method

SOLUTION NMR