Structural clues to Rab GTPase functional diversity.
Rab GTPases are key regulators of membrane trafficking in eukaryotes. Recent structural analysis of a number of Rabs, either alone or in complex with partner proteins, has provided new insight into the importance of both conserved and non-conserved features of these proteins that specify their unique functions and localizations. This review will highlight what we have learned from crystallographic analysis of this important protein family.
Pfeffer
Suzanne R
SR
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305-5307, USA. pfeffer@stanford.edu
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D017124:Conserved Sequence; D019143:Evolution, Molecular; D006801:Humans; D008969:Molecular Sequence Data; D015394:Molecular Structure; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship; D015003:Yeasts / Q000235:genetics / Q000502:physiology; D020691:rab GTP-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology
D020691:rab GTP-Binding Proteins