Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein.
The 1.8 A crystal structure of transducin alpha.GDP, when compared to that of the activated complex with GTP-gamma S, reveals the nature of the conformational changes that occur on activation of a heterotrimeric G-protein alpha-subunit. Structural changes initiated by direct contacts with the terminal phosphate of GTP propagate to regions that have been implicated in effector activation. The changes are distinct from those observed in other members of the GTPase superfamily.
Lambright
D G
DG
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510.
Noel
J P
JP
Hamm
H E
HE
Sigler
P B
PB
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D006153:Guanosine Diphosphate / Q000737:chemistry; D006160:Guanosine Triphosphate / Q000737:chemistry; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D010444:Peptide Elongation Factor Tu / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D016283:Proto-Oncogene Proteins p21(ras) / Q000737:chemistry; D012374:Rod Cell Outer Segment / Q000737:chemistry; D013329:Structure-Activity Relationship; D015293:Transducin / Q000737:chemistry*
D010446:Peptide Fragments; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu; D015293:Transducin; C501009:HRAS protein, human; D016283:Proto-Oncogene Proteins p21(ras)