Publication Abstract from PubMed
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. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: SEPT7G and SEPT7Gbind by X-ray crystallography (View interaction). SEPT7 G and SEPT7 Gbind by molecular sieving (View interaction).
Promiscuous interactions of human septins: The GTP binding domain of SEPT7 forms filaments within the crystal.,Serrao VH, Alessandro F, Caldas VE, Marcal RL, D'Muniz Pereira H, Thiemann OH, Garratt RC FEBS Lett. 2011 Nov 3. PMID:22064074[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
