TY - JOUR
T1 - G proteins, effecters and GAPs
T2 - Structure and mechanism
AU - Sprang, Stephen R.
N1 - Funding Information:
1 thank Mark Wall for assistance in the production of figures. Research has been supported in part by grants from the National Institutes of Health
PY - 1997/12
Y1 - 1997/12
N2 - G proteins form a diverse family of regulatory GTPases which, in the GTP-bound state, bind to and activate downstream effecters. Structures of Ras homologs bound to effector domains have revealed mechanisms by which G proteins couple GTP binding to effector activation and achieve specificity. Complexes between structurally unrelated GTPase-activating proteins with complementary G proteins suggest common mechanisms by which GTP hydrolysis is stimulated via direct interactions with conformationally labile switch regions of the G protein.
AB - G proteins form a diverse family of regulatory GTPases which, in the GTP-bound state, bind to and activate downstream effecters. Structures of Ras homologs bound to effector domains have revealed mechanisms by which G proteins couple GTP binding to effector activation and achieve specificity. Complexes between structurally unrelated GTPase-activating proteins with complementary G proteins suggest common mechanisms by which GTP hydrolysis is stimulated via direct interactions with conformationally labile switch regions of the G protein.
UR - http://www.scopus.com/inward/record.url?scp=0031283407&partnerID=8YFLogxK
U2 - 10.1016/S0959-440X(97)80157-1
DO - 10.1016/S0959-440X(97)80157-1
M3 - Article
C2 - 9434906
AN - SCOPUS:0031283407
SN - 0959-440X
VL - 7
SP - 849
EP - 856
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 6
ER -