Interactions between conserved residues in transmembrane helices 2 and 7 during angiotensin AT1 receptor activation.

@article{Nikiforovich2006InteractionsBC,
  title={Interactions between conserved residues in transmembrane helices 2 and 7 during angiotensin AT1 receptor activation.},
  author={Gregory V. Nikiforovich and Meng Zhang and Qing Yang and Gowraganahalli Jagadeesh and Hao-Chia Chen and L{\'a}szl{\'o} Hunyady and Garland R. Marshall and Kevin J. Catt},
  journal={Chemical biology & drug design},
  year={2006},
  volume={68 5},
  pages={239-49}
}
Site-directed mutagenesis studies and independent molecular modeling studies were combined to investigate the network of inter-residue interactions within the transmembrane region of the angiotensin AT(1a) receptor. Site-directed mutagenesis was focused on residues Tyr292, Asn294, Asn295, and Asn298 in transmembrane helix 7, and the conserved Asp74 in helix 2 and other polar residues. Functional interactions between pairs of residues were evaluated by determining the effects of single and… CONTINUE READING

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Critical role of a conserved intramembrane tyrosine residue in angiotensin II receptor activation

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