| Autor: |
Yee DK; Department of Animal Biology, Institute of Neurological Sciences, University of Pennsylvania, Philadelphia 19104, USA., Kisley LR, Heerding JN, Fluharty SJ |
| Jazyk: |
angličtina |
| Zdroj: |
Brain research. Molecular brain research [Brain Res Mol Brain Res] 1997 Nov; Vol. 51 (1-2), pp. 238-41. |
| DOI: |
10.1016/s0169-328x(97)00244-1 |
| Abstrakt: |
A fifth transmembrane domain lysine residue is conserved in both the type 1 (AT1) and type 2 (AT2) angiotensin II (AngII) receptors. This lysine (Lys199) is believed to play a critical role in peptide binding for the AT1 receptor. To evaluate its possible role in the AT2 receptor, the analogous AT2 residue (Lys199) was changed to glutamine. This mutation greatly reduced the affinity for both 125I-AngII and 125I-Sar1,Ile8-AngII and abolished binding to the non-peptide 125I-PD122979. These data indicate that despite a relatively low homology of 34%, some commonalities in the binding mechanism for AngII may exist between the two subtypes. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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