PMID- 8266082
OWN - NLM
STAT- MEDLINE
DCOM- 19940121
LR  - 20190618
IS  - 0036-8075 (Print)
IS  - 0036-8075 (Linking)
VI  - 262
IP  - 5141
DP  - 1993 Dec 17
TI  - Separate GTP binding and GTPase activating domains of a G alpha subunit.
PG  - 1895-901
AB  - Most members of the guanosine triphosphatase (GTPase) superfamily hydrolyze 
      guanosine triphosphate (GTP) quite slowly unless stimulated by a GTPase 
      activating protein or GAP. The alpha subunits (G alpha) of the heterotrimeric G 
      proteins hydrolyze GTP much more rapidly and contain an approximately 120-residue 
      insert not found in other GTPases. Interactions between a G alpha insert domain 
      and a G alpha GTP-binding core domain, both expressed as recombinant proteins, 
      show that the insert acts biochemically as a GAP. The results suggest a general 
      mechanism for GAP-dependent hydrolysis of GTP by other GTPases.
FAU - Markby, D W
AU  - Markby DW
AD  - Department of Pharmcology, University of California, San Francisco 94143.
FAU - Onrust, R
AU  - Onrust R
FAU - Bourne, H R
AU  - Bourne HR
LA  - eng
GR  - 5F32-GM13918/GM/NIGMS NIH HHS/United States
GR  - CA54427/CA/NCI NIH HHS/United States
GR  - GM27800/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Science
JT  - Science (New York, N.Y.)
JID - 0404511
RN  - 1F7A44V6OU (Colforsin)
RN  - 37589-80-3 (Guanosine 5'-O-(3-Thiotriphosphate))
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - E0399OZS9N (Cyclic AMP)
RN  - EC 3.6.1.- (GTP Phosphohydrolases)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
RN  - EC 4.6.1.1 (Adenylyl Cyclases)
SB  - IM
MH  - Adenylyl Cyclases/metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cell Line
MH  - Colforsin/pharmacology
MH  - Cyclic AMP/metabolism
MH  - GTP Phosphohydrolases/*metabolism
MH  - GTP-Binding Proteins/chemistry/*metabolism
MH  - Guanosine 5'-O-(3-Thiotriphosphate)/metabolism/pharmacology
MH  - Guanosine Triphosphate/*metabolism
MH  - Hydrolysis
MH  - Kinetics
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Protein Conformation
EDAT- 1993/12/17 00:00
MHDA- 1993/12/17 00:01
CRDT- 1993/12/17 00:00
PHST- 1993/12/17 00:00 [pubmed]
PHST- 1993/12/17 00:01 [medline]
PHST- 1993/12/17 00:00 [entrez]
AID - 10.1126/science.8266082 [doi]
PST - ppublish
SO  - Science. 1993 Dec 17;262(5141):1895-901. doi: 10.1126/science.8266082.