Gs alpha meets its target--shedding light on a key signal transduction event

J J Dumas; D G Lambright

doi:10.1016/s0969-2126(98)00042-2

Gs alpha meets its target--shedding light on a key signal transduction event

Structure. 1998 Apr 15;6(4):407-11. doi: 10.1016/s0969-2126(98)00042-2.

Authors

J J Dumas¹, D G Lambright

Affiliation

¹ Program in Molecular Medicine, University of Massachusetts Medical Center, 373 Plantation Street, Worcester, MA 01605, USA.

PMID: 9562564
DOI: 10.1016/s0969-2126(98)00042-2

Abstract

The recently determined crystal structure of Gs alpha bound to a catalytically active form of adenylyl cyclase reveals the location of the enzyme's active site and provides the first view of heterotrimeric G protein alpha subunit activating a downstream effector. Comparison with the structure of a catalytically inactive form of adenylyl cyclase suggests a plausible allosteric mechanism whereby the synergistic activators Gs alpha and forskolin stimulate the activity of adenylyl cyclase.

Publication types

Review

MeSH terms

Adenosine Triphosphate / chemistry
Adenylyl Cyclases / chemistry*
Allosteric Regulation / physiology
Binding Sites / physiology
GTP-Binding Protein alpha Subunits, Gs / chemistry*
Guanosine Triphosphate / chemistry
Models, Molecular
Protein Conformation
Signal Transduction / physiology*

Substances

Guanosine Triphosphate
Adenosine Triphosphate
GTP-Binding Protein alpha Subunits, Gs
Adenylyl Cyclases