1go5: Difference between revisions
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{{STRUCTURE_1go5| PDB=1go5 | SCENE= }} | |||
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'''STRUCTURE OF THE C-TERMINAL FG-BINDING DOMAIN OF HUMAN TAP''' | '''STRUCTURE OF THE C-TERMINAL FG-BINDING DOMAIN OF HUMAN TAP''' | ||
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[[Category: Neuhaus, D.]] | [[Category: Neuhaus, D.]] | ||
[[Category: Stewart, M.]] | [[Category: Stewart, M.]] | ||
[[Category: | [[Category: Mrna export]] | ||
[[Category: | [[Category: Nuclear transport]] | ||
[[Category: | [[Category: Nucleoporin]] | ||
[[Category: | [[Category: Uba]] | ||
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Revision as of 14:48, 2 May 2008
STRUCTURE OF THE C-TERMINAL FG-BINDING DOMAIN OF HUMAN TAP
Overview
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.
About this Structure
1GO5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 17:48:46 2008
