Abstract：
:The nuclear pore complex is the sole mediator of bidirectional transport between the nucleus and cytoplasm. Nup358 is a metazoan-specific nucleoporin that localizes to the cytoplasmic filaments and provides several binding sites for the mobile nucleocytoplasmic transport machinery. Here we present the crystal structure of the C-terminal domain (CTD) of Nup358 at 1.75Å resolution. The structure reveals that the CTD adopts a cyclophilin-like fold with a non-canonical active-site configuration. We determined biochemically that the CTD possesses weak peptidyl-prolyl isomerase activity and show that the active-site cavity mediates a weak association with the human immunodeficiency virus-1 capsid protein, supporting its role in viral infection. Overall, the surface is evolutionarily conserved, suggesting that the CTD serves as a protein-protein interaction platform. However, we demonstrate that the CTD is dispensable for nuclear envelope localization of Nup358, suggesting that the CTD does not interact with other nucleoporins.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Lin DH,Zimmermann S,Stuwe T,Stuwe E,Hoelz Adoi
10.1016/j.jmb.2013.01.021subject
Has Abstractpub_date
2013-04-26 00:00:00pages
1318-29issue
8eissn
0022-2836issn
1089-8638pii
S0022-2836(13)00037-5journal_volume
425pub_type
杂志文章abstract：:A hydrogen exchange (HX) functional labeling method was used to study allosterically active segments in human hemoglobin (Hb) at the alpha-chain N terminus and the beta-chain C terminus. Allosterically important interactions that contact these segments were removed one or more at a time by mutation (Hbs Cowtown, Bunbu...
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journal_title：Journal of molecular biology
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