1go5
From Proteopedia
Structure of the C-terminal FG-binding domain of human Tap
Structural highlights
FunctionNXF1_HUMAN Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm. The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5.[1] [2] Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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