Primary structure of the α‐subunit of bovine adenylate cyclase‐stimulating G‐protein deduced from the cDNA sequence
Первичная структура α-субъединицы стимулирующего аденилатциклазу G-белка крупного рогатого скота, выведенная на основе последовательности кДНК
1986-01-20
SCID: 54.1/qzjg43hr
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Gs alpha-subunitadenylate cyclasecDNA sequenceelongation factor-Tuguanine nucleotide-binding proteins
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Abstract (AI)
The primary structure of the alpha-subunit of the adenylate cyclase-stimulating G-protein (Gs) has been deduced from the nucleotide sequence of cloned DNA complementary to the bovine cerebral mRNA encoding the polypeptide. Comparison of the amino acid sequences of the alpha-subunits of Gs and transducin reveals that some of the highly conserved regions show sequence homology with elongation factor-Tu and ras p21 proteins and correspond to functional regions of guanine nucleotide-binding proteins.
Key Findings
1
Comparison with transducin α-subunit sequences identified highly conserved regions shared among these guanine nucleotide-binding proteins.
2
Several conserved Gs and transducin regions show homology to elongation factor-Tu and ras p21 proteins.
3
The primary amino acid structure of the bovine adenylate cyclase-stimulating G-protein α-subunit was deduced from a cloned cDNA sequence.
4
These homologous regions correspond to functional domains involved in guanine nucleotide binding.
Research Object
the alpha-subunit of the adenylate cyclase-stimulating G-protein (Gs) from bovine brain
Research Subject
the primary amino acid structure and conserved, functionally relevant guanine-nucleotide-binding regions of the Gs alpha-subunit
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1986-01-20
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