1go5

From Proteopedia

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Revision as of 15:01, 12 November 2007

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STRUCTURE OF THE C-TERMINAL FG-BINDING DOMAIN OF HUMAN TAP

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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.

Disease

Known diseases associated with this structure: Bare lymphocyte syndrome, type I OMIM:[170260]

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

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