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TY - JOUR AU - Noel, Joseph P. AU - Hamm, Heidi E. AU - Sigler, Paul B. PY - 1993 DA - 1993/12/01 TI - The 2.2 Å crystal structure of transducin-α complexed with GTPγS JO - Nature SP - 654 EP - 663 VL - 366 IS - 6456 AB - The 2.2 Å crystal structure of activated rod transducin, Gtα-GTPγS, shows the bound GTPγS molecule occluded deep in a cleft between a domain structurally homologous to small GTPases and a helical domain unique to heterotrimeric G proteins. The structure, when combined with biochemical and genetic studies, suggests: how an activated receptor might open this cleft to allow nucleotide exchange; a mechanism for GTP-induced changes in effector and receptor binding surfaces; and a mechanism for GTPase activity not evident from previous data. SN - 1476-4687 UR - https://doi.org/10.1038/366654a0 DO - 10.1038/366654a0 ID - Noel1993 ER -