Glycyl-histidyl-lysine interacts with the angiotensin II AT1 receptor
✍ Scribed by J.Adolfo García-Sáinz; J.Alberto Olivares-Reyes
- Book ID
- 116113465
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 561 KB
- Volume
- 16
- Category
- Article
- ISSN
- 0196-9781
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The carboxyl-terminal cytoplasmic domain of the angiotensin II type 1 receptor (AT1) is known to interact with several classes of intracellular proteins that may modulate receptor function. Employing yeast two-hybrid screening of a human embryonic kidney cDNA library with the carboxyl-terminal cytop
## Abstract Interaction between angiotensin II (Ang II) and the fragment peptide 300–320 (__fCT__^__300–320__^) of the rat angiotensin II receptor AT~1a~ was demonstrated by relaxation measurements, NOE effects, chemical shift variations, and CD measurements. The correlation times modulating dipola