Structure-binding studies of the adrenal AT4 receptor: analysis of position two- and three-modified angiotensin IV analogs.
Amino acid substitutions in positions two and three of angiotensin IV (VYIHPF) were carried out to determine which structural features of the side-chains were important for achieving high-affinity binding to bovine adrenal receptors. These studies demonstrated that an activated aromatic ring in the second position side-chain resulted in the highest-affinity binding. Position three required a hydrophobic amino acid to achieve high-affinity binding. Both aliphatic and aromatic side-chains were sufficient to yield high-affinity binding.
Krishnan
R
R
Department of VCAPP, Washington State University, Pullman 99164-6520, USA.
Hanesworth
J M
JM
Wright
J W
JW
Harding
J W
JW
D000311:Adrenal Glands / Q000378:metabolism*; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000804:Angiotensin II / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D002417:Cattle; D011485:Protein Binding; D011945:Receptors, Angiotensin / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship
D011945:Receptors, Angiotensin; D000804:Angiotensin II; C012877:angiotensin II, des-Asp(1)-des-Arg(2)-Ile(5)-