期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 80, 期 8, 页码 2110-2116出版社
WILEY
DOI: 10.1002/prot.24102
关键词
nuclear pore complex; Nup116; Nup98; Nup100; Nup145; mRNA export; structural genomics
资金
- NIH [U01 GM098256, U54 GM074945, U54 GM094662, NIH R01 GM062427, NIH R01 GM083960, NIH U54 RR022220]
- US Department of Energy, Office of Basic Energy Sciences
- DOE Office of Biological and Environmental Research
- National Institutes of Health, National Center for Research Resources, Biomedical Technology Program [P41RR001209]
The nuclear pore complex (NPC), embedded in the nuclear envelope, is a large, dynamic molecular assembly that facilitates exchange of macromolecules between the nucleus and the cytoplasm. The yeast NPC is an eightfold symmetric annular structure composed of similar to 456 polypeptide chains contributed by similar to 30 distinct proteins termed nucleoporins. Nup116, identified only in fungi, plays a central role in both protein import and mRNA export through the NPC. Nup116 is a modular protein with N-terminal FG repeats containing a Gle2p-binding sequence motif and a NPC targeting domain at its C-terminus. We report the crystal structure of the NPC targeting domain of Candida glabrata Nup116, consisting of residues 8821034 [CgNup116(8821034)], at 1.94 angstrom resolution. The X-ray structure of CgNup116(8821034) is consistent with the molecular envelope determined in solution by small-angle X-ray scattering. Structural similarities of CgNup116(8821034) with homologous domains from Saccharomyces cerevisiae Nup116, S. cerevisiae Nup145N, and human Nup98 are discussed. Proteins 2012; (c) 2012 Wiley Periodicals, Inc.
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