title: Structure-binding studies of the adrenal AT4 receptor: analysis of position two- and three-modified angiotensin IV analogs.
abstract: 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.
authors.affiliation: Department of VCAPP, Washington State University, Pullman 99164-6520, USA.
authors.forename: R
authors.initials: R
authors.lastname: Krishnan
authors.forename: J M
authors.initials: JM
authors.lastname: Hanesworth
authors.forename: J W
authors.initials: JW
authors.lastname: Wright
authors.forename: J W
authors.initials: JW
authors.lastname: Harding
mesh_terms: 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
chemical_list: D011945:Receptors, Angiotensin; D000804:Angiotensin II; C012877:angiotensin II, des-Asp(1)-des-Arg(2)-Ile(5)-