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1GO5

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

Summary for 1GO5
Entry DOI10.2210/pdb1go5/pdb
Related1FO1
NMR InformationBMRB: 5364
DescriptorTIP ASSOCIATING PROTEIN (1 entity in total)
Functional Keywordsnuclear transport, mrna export, uba, nucleoporins
Biological sourceHOMO SAPIENS (HUMAN)
Total number of polymer chains1
Total formula weight7718.60
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 citationGrant, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2024-11-06公开中

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