Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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
