Photolabelling implicates an amino acid in the second transmembrane domain of the rat AT1A receptor in agonist binding.
Bajaj
B P
BP
Institute For Cardiovascular Research, University of Leeds, U.K.
Balmforth
A J
AJ
Ball
S G
SG
D000345:Affinity Labels; D000803:Angiotensin I / Q000378:metabolism*; D000804:Angiotensin II / Q000031:analogs & derivatives* / Q000378:metabolism*; D000818:Animals; D001386:Azides / Q000378:metabolism*; D002460:Cell Line; D010450:Endopeptidases; D019204:GTP-Binding Proteins / Q000378:metabolism; D006801:Humans; D007668:Kidney; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D051381:Rats; D011945:Receptors, Angiotensin / Q000737:chemistry* / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D014162:Transfection
D000345:Affinity Labels; D001386:Azides; D010446:Peptide Fragments; D011945:Receptors, Angiotensin; D011994:Recombinant Proteins; C093703:angiotensin II, Sar(1)-Ile(5)-(4-azido)Phe(8)-; D000804:Angiotensin II; D000803:Angiotensin I; D010450:Endopeptidases; D019204:GTP-Binding Proteins