Multiple binding modes for the receptor-bound conformations of cyclic AII agonists.

@article{Pluciska1993MultipleBM,
  title={Multiple binding modes for the receptor-bound conformations of cyclic AII agonists.},
  author={Krystyna Plucińska and Takahiro Kataoka and Mitsuaki Yodo and Wayne Livingston Cody and J X He and Christine Humblet and Gina H. Lu and Elizabeth A. Lunney and Terry C Major and Robert L. Panek},
  journal={Journal of medicinal chemistry},
  year={1993},
  volume={36 13},
  pages={
          1902-13
        }
}
Angiotensin II, Asp-Arg-Val-Tyr-His-Pro-Phe, binds its receptor with a postulated turn centered at residue four. Analogs of angiotensin II which contain a disulfide bridge between the side chains of residues 3 and 5 retain significant activity consistent with this hypothesis. Incorporation of 4-mercaptoproline residues, a hybrid, or chimeric amino acid which combines the properties of proline and homocysteine, into either of these positions with analogous disulfide bridges allows retention of… 
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Design, synthesis, and biological activities of four angiotensin II receptor ligands with gamma-turn mimetics replacing amino acid residues 3-5.
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Con conformational analysis studies using theoretical calculations and 1H-NMR spectroscopy on tripeptide model compounds of these cyclic octapeptides show that the cyclic moieties of c[Cys3,5]-Ang II and c[Pen3, 5]- Ang II preferentially assume an inverse gamma-turn conformation.
Conformational analysis of two cyclic analogs of angiotensin: implications for the biologically active conformation.
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These conformers of cyclo[Sar1, Cys3, Mpt5]-AT contain "an open turn" in the backbone of the Tyr4-Val5 residues, instead of the earlier proposed beta-like reversal, thus confirming the suggestion that the conformation(s) ensuring binding of AT analogs with specific receptors should not be described in terms of a unique backbone conformer.
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It is concluded that the 1,3,5-trisubstituted benzene rings can be conveniently prepared and are suitable as gamma-turn mimics and a tentative agonist model is proposed for AT2 receptor activation by angiotensin II analogues.
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The present study investigates the importance of the amino acid side chains in the octapeptide angiotensin II (Ang II) for binding to the AT2 receptor and synthesized some N-terminally modified Ang II analogues to investigate the role of the Arg2 side chain for receptor binding.
Vinyl sulfide cyclized analogues of angiotensin II with high affinity and full agonist activity at the AT(1) receptor.
TLDR
The cyclic vinyl sulfides that have agonist activity were both shown to possess low-energy conformers compatible with the previously proposed 3D model for the bioactive conformation of Ang II.
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