PMID- 9395396
OWN - NLM
STAT- MEDLINE
DCOM- 19971224
LR  - 20190618
IS  - 0036-8075 (Print)
IS  - 0036-8075 (Linking)
VI  - 278
IP  - 5345
DP  - 1997 Dec 12
TI  - Crystal structure of the adenylyl cyclase activator Gsalpha.
PG  - 1943-7
AB  - The crystal structure of Gsalpha, the heterotrimeric G protein alpha subunit that 
      stimulates adenylyl cyclase, was determined at 2.5 A in a complex with guanosine 
      5'-O-(3-thiotriphosphate) (GTPgammaS). Gsalpha is the prototypic member of a 
      family of GTP-binding proteins that regulate the activities of effectors in a 
      hormone-dependent manner. Comparison of the structure of Gsalpha.GTPgammaS with 
      that of Gialpha.GTPgammaS suggests that their effector specificity is primarily 
      dictated by the shape of the binding surface formed by the switch II helix and 
      the alpha3-beta5 loop, despite the high sequence homology of these elements. In 
      contrast, sequence divergence explains the inability of regulators of G protein 
      signaling to stimulate the GTPase activity of Gsalpha. The betagamma binding 
      surface of Gsalpha is largely conserved in sequence and structure to that of 
      Gialpha, whereas differences in the surface formed by the carboxyl-terminal helix 
      and the alpha4-beta6 loop may mediate receptor specificity.
FAU - Sunahara, R K
AU  - Sunahara RK
AD  - Department of Pharmacology, The University of Texas Southwestern Medical Center, 
      5323 Harry Hines Boulevard, Dallas, TX 75235-9041, USA.
FAU - Tesmer, J J
AU  - Tesmer JJ
FAU - Gilman, A G
AU  - Gilman AG
FAU - Sprang, S R
AU  - Sprang SR
LA  - eng
SI  - PDB/1AZT
GR  - DK46371/DK/NIDDK NIH HHS/United States
GR  - GM34497/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  - 37589-80-3 (Guanosine 5'-O-(3-Thiotriphosphate))
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - EC 3.6.1.- (GTP Phosphohydrolases)
RN  - EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, Gi-Go)
RN  - EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, Gs)
RN  - EC 4.6.1.1 (Adenylyl Cyclases)
RN  - I38ZP9992A (Magnesium)
SB  - IM
CIN - Science. 1997 Dec 12;278(5345):1898-9. PMID: 9417637
MH  - Adenylyl Cyclases/chemistry/*metabolism
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Conserved Sequence
MH  - Crystallization
MH  - Crystallography, X-Ray
MH  - Dimerization
MH  - Enzyme Activation
MH  - GTP Phosphohydrolases/metabolism
MH  - GTP-Binding Protein alpha Subunits, Gi-Go/chemistry/metabolism
MH  - GTP-Binding Protein alpha Subunits, Gs/*chemistry/metabolism
MH  - Guanosine 5'-O-(3-Thiotriphosphate)/*chemistry/metabolism
MH  - Guanosine Triphosphate/metabolism
MH  - Hydrolysis
MH  - Magnesium/metabolism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - *Protein Conformation
MH  - Protein Structure, Secondary
MH  - Signal Transduction
EDAT- 1998/01/07 00:00
MHDA- 1998/01/07 00:01
CRDT- 1998/01/07 00:00
PHST- 1998/01/07 00:00 [pubmed]
PHST- 1998/01/07 00:01 [medline]
PHST- 1998/01/07 00:00 [entrez]
AID - 10.1126/science.278.5345.1943 [doi]
PST - ppublish
SO  - Science. 1997 Dec 12;278(5345):1943-7. doi: 10.1126/science.278.5345.1943.