Structure-binding studies of the adrenal AT(4) receptor: analysis of position two- and three-modified angiotensin IV analogs

Authors
Krishnan, R Hanesworth, JM Wright, JW Harding, JW
Citation
R. Krishnan et al., Structure-binding studies of the adrenal AT(4) receptor: analysis of position two- and three-modified angiotensin IV analogs, PEPTIDES, 20(8), 1999, pp. 915-920
Citations number
17
Categorie Soggetti
Biochemistry & Biophysics
Journal title
PEPTIDES
ISSN journal
01969781 → ACNP
Volume
20
Issue
8
Year of publication
1999
Pages
915 - 920
Database
ISI
SICI code
0196-9781(1999)20:8<915:SSOTAA>2.0.ZU;2-P
Abstract
Amino acid substitutions in positions two and three of angiotensin IV (VYIH PF) were carried out to determine which structural features of the side-cha ins were important for achieving high-affinity binding to bovine adrenal re ceptors. These studies demonstrated that an activated aromatic ring in the second position side-chain resulted in the highest-affinity binding. Positi on three required a hydrophobic amino acid to achieve high-affinity binding . Both aliphatic and aromatic side-chains were sufficient to yield high-aff inity binding. (C) 1999 Elsevier Science Inc. All rights reserved.