Allosteric modulation of nucleoporin assemblies by intrinsically disordered regions
Copyright policy )Allosteric modulation of nucleoporin assemblies by intrinsically disordered regions
Kap121 interacts with an intrinsically disordered region of Nup53 to allosterically modulate Nup53 binding to partner nucleoporins.
- Seoul National University Korea (Republic of)
- Harvard University United States
- Dana-Farber Cancer Institute United States
- Rockefeller University United States
- Howard Hughes Medical Institute United States
STRUCTURAL BASIS, Saccharomyces cerevisiae Proteins, PROTEINS, MOLECULAR ARCHITECTURE, NUCLEAR-PORE COMPLEX, TITRATION, Receptors, Cytoplasmic and Nuclear, 612, Saccharomyces cerevisiae, CHANNEL, Allosteric Regulation, Protein Domains, BINDING, Research Articles, KAP121P, Science & Technology, INNER RING, Membrane Transport Proteins, DNA, Multidisciplinary Sciences, Intrinsically Disordered Proteins, Nuclear Pore Complex Proteins, Multiprotein Complexes, Nuclear Pore, Science & Technology - Other Topics
STRUCTURAL BASIS, Saccharomyces cerevisiae Proteins, PROTEINS, MOLECULAR ARCHITECTURE, NUCLEAR-PORE COMPLEX, TITRATION, Receptors, Cytoplasmic and Nuclear, 612, Saccharomyces cerevisiae, CHANNEL, Allosteric Regulation, Protein Domains, BINDING, Research Articles, KAP121P, Science & Technology, INNER RING, Membrane Transport Proteins, DNA, Multidisciplinary Sciences, Intrinsically Disordered Proteins, Nuclear Pore Complex Proteins, Multiprotein Complexes, Nuclear Pore, Science & Technology - Other Topics
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