Promiscuous interactions of human septins: The GTP binding domain of SEPT7 forms filaments within the crystal
Copyright policy )Promiscuous interactions of human septins: The GTP binding domain of SEPT7 forms filaments within the crystal
We describe the purification, crystallization and structure for the GTP-binding domain of human septin 7 (SEPT7G). We show that it forms filaments within the crystal lattice which employ both the G and NC interfaces, similar to those seen in the hetero-filament of SEPT2/6/7. The NC interface is considered promiscuous as it is absent from the hetero-filament. Such promiscuity could provide the potential for permuting monomers along a filament in order to generate diversity in hetero-polymers. On the other hand, our results suggest that the G and NC interfaces may be necessary but insufficient for determining correct hetero-filament assembly.
Models, Molecular, Subunit interface, Cell Cycle Proteins, Crystallography, X-Ray, GTP-binding domain, Protein Structure, Tertiary, Substrate Specificity, Protein Subunits, Promiscuous interaction, SEPT7, Filament, Humans, Septin, Guanosine Triphosphate, Septins
Models, Molecular, Subunit interface, Cell Cycle Proteins, Crystallography, X-Ray, GTP-binding domain, Protein Structure, Tertiary, Substrate Specificity, Protein Subunits, Promiscuous interaction, SEPT7, Filament, Humans, Septin, Guanosine Triphosphate, Septins
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