Literature summary for 4.6.1.1 extracted from

Tong, R.; Wade, R.; Bruce, N.
Comparative electrostatic analysis of adenylyl cyclase for isoform dependent regulation properties (2016), Proteins, 84, 1844-1858 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
homology modeling and comparative electrostatic analysis of the catalytic domains of all nine transmembrane adenylate cyclase isoforms providing support for the positioning of the binding site of the inhibitory protein Gialpha at a pseudo-symmetric position to the stimulatory Gsalpha binding site, a structural interpretation of the Gbetacamma interaction with adenylae cyclases 2, 4, and 7 and a new binding site for RGS2	Mus musculus

Crystallization (Comment)

Organism

homology modeling and comparative electrostatic analysis of the catalytic domains of all nine transmembrane adenylate cyclase isoforms providing support for the positioning of the binding site of the inhibitory protein Gialpha at a pseudo-symmetric position to the stimulatory Gsalpha binding site, a structural interpretation of the Gbetacamma interaction with adenylae cyclases 2, 4, and 7 and a new binding site for RGS2

Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	O88444	isoform Adcy1	-
Mus musculus	P51829	isoform Adcy7	-
Mus musculus	P51830	isoform Adcy9	-
Mus musculus	P84309	isoform Adcy5	-
Mus musculus	P97490	isoform Adcy8	-
Mus musculus	Q01341	isoform Adcy6	-
Mus musculus	Q80TL1	isoform Adcy2	-
Mus musculus	Q8VHH7	isoform Adcy3	-
Mus musculus	Q91WF3	isoform Adcy4	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)