Structural flexibility of small GTPases. Can it explain their functional versatility?
Multiple interactions with many different partners are responsible for the amazing functional versatility of proteins, especially those participating in cellular regulation. The structural properties that could facilitate multiple interactions are examined for small GTPases. The role of cellular constraints, compartmentation and scaffolds on protein-protein interactions is considered.
Helmreich
Ernst J M
EJ
The Biocenter of the University of Würzburg, Am Hubland, D-97074 Würzburg, Germany. e.helmreich@mail.uni-wuerzburg.de
D000818:Animals; D020558:GTP Phosphohydrolases / Q000737:chemistry* / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000378:metabolism; D011905:Genes, ras / Q000502:physiology; D006801:Humans; D008958:Models, Molecular; D008970:Molecular Weight; D019869:Phosphatidylinositol 3-Kinases / Q000378:metabolism; D019908:Proto-Oncogene Proteins c-raf / Q000502:physiology; D020239:Receptor Cross-Talk / Q000502:physiology; D020931:ran GTP-Binding Protein / Q000502:physiology
D019869:Phosphatidylinositol 3-Kinases; D019908:Proto-Oncogene Proteins c-raf; D020558:GTP Phosphohydrolases; D019204:GTP-Binding Proteins; D020931:ran GTP-Binding Protein