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Structure-binding studies of the adrenal AT4 receptor: analysis of position two- and three-modified angiotensin IV
R Krishnan1, J M Hanesworth, J W Wright
1Department of VCAPP, Washington State University, Pullman 99164-6520, USA.
Peptides
|September 30, 1999
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.