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1go5
From Proteopedia
| 1go5, 26 NMR models () | |||||||||
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| Domains: | TAP_C | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
STRUCTURE OF THE C-TERMINAL FG-BINDING DOMAIN OF HUMAN TAP
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.
Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1., Grant RP, Hurt E, Neuhaus D, Stewart M, Nat Struct Biol. 2002 Apr;9(4):247-51. PMID:11875519
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1GO5 is a 1 chain structure of sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
- Grant RP, Hurt E, Neuhaus D, Stewart M. Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1. Nat Struct Biol. 2002 Apr;9(4):247-51. PMID:11875519 doi:10.1038/nsb773
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