P2U purinoceptors: cDNA cloning, signal transduction mechanisms and structure-function analysis.
The cloning of a P2U purinoceptor cDNA has made it possible to use molecular biological approaches to investigate P2U purinoceptor function. Expression of recombinant P2U purinoceptors in mammalian cells lacking endogenous P2U purinoceptors has enabled us to characterize the receptor protein and its downstream effectors, and has allowed a partial analysis of the role of certain amino acid residues in ligand binding. These approaches have placed the pharmacological classification of the P2U purinoceptor on a firm molecular footing and have generated model systems that can be used to investigate receptor-ligand binding, regulation and signal transduction.
Lustig
K D
KD
Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Weisman
G A
GA
Turner
J T
JT
Garrad
R
R
Shiau
A K
AK
Erb
L
L
D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D018076:DNA, Complementary; D006801:Humans; D008969:Molecular Sequence Data; D018048:Receptors, Purinergic P2 / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D058473:Receptors, Purinergic P2Y2; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction / Q000502:physiology*; D013329:Structure-Activity Relationship
D018076:DNA, Complementary; C546385:P2RY2 protein, human; D018048:Receptors, Purinergic P2; D058473:Receptors, Purinergic P2Y2