2v75
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N-TERMINAL DOMAIN OF NAB2
OverviewOverview
Nuclear abundant poly(A) RNA-binding protein 2 (Nab2) is an essential, yeast heterogeneous nuclear ribonucleoprotein that modulates both mRNA, nuclear export and poly(A) tail length. The N-terminal domain of Nab2, (residues 1-97) mediates interactions with both the C-terminal globular, domain of the nuclear pore-associated protein, myosin-like protein 1, (Mlp1), and the mRNA export factor, Gfd1. The solution and crystal, structures of the Nab2 N-terminal domain show a primarily helical fold, that is analogous to the PWI fold found in several other RNA-binding, proteins. In contrast to other PWI-containing proteins, we find no, evidence that the Nab2 N-terminal domain binds to nucleic acids. Instead, this domain appears to mediate protein:protein interactions that, facilitate the nuclear export of mRNA. The Nab2 N-terminal domain has a, distinctive hydrophobic patch centered on Phe73, consistent with this, region of the surface being a protein:protein interaction site. Engineered, mutations within this hydrophobic patch attenuate the interaction with the, Mlp1 C-terminal domain but do not alter the interaction with Gfd1, indicating that this patch forms a crucial component of the interface, between Nab2 and Mlp1.
About this StructureAbout this Structure
2V75 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the N-Terminal Mlp1-Binding Domain of the Saccharomyces cerevisiae mRNA-Binding Protein, Nab2., Grant RP, Marshall NJ, Yang JC, Fasken MB, Kelly SM, Harreman MT, Neuhaus D, Corbett AH, Stewart M, J Mol Biol. 2007 Dec 4;. PMID:18190927
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