Autor: |
Kobilka, B K, Dixon, R A, Frielle, T, Dohlman, H G, Bolanowski, M A, Sigal, I S, Yang-Feng, T L, Francke, U, Caron, M G, Lefkowitz, R J |
Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; January 1987, Vol. 84 Issue: 1 p46-50, 5p |
Abstrakt: |
We have isolated and sequenced a cDNA encoding the human beta 2-adrenergic receptor. The deduced amino acid sequence (413 residues) is that of a protein containing seven clusters of hydrophobic amino acids suggestive of membrane-spanning domains. While the protein is 87% identical overall with the previously cloned hamster beta 2-adrenergic receptor, the most highly conserved regions are the putative transmembrane helices (95% identical) and cytoplasmic loops (93% identical), suggesting that these regions of the molecule harbor important functional domains. Several of the transmembrane helices also share lesser degrees of identity with comparable regions of select members of the opsin family of visual pigments. We have localized the gene for the beta 2-adrenergic receptor to q31-q32 on chromosome 5. This is the same position recently determined for the gene encoding the receptor for platelet-derived growth factor and is adjacent to that for the FMS protooncogene, which encodes the receptor for the macrophage colony-stimulating factor. |
Databáze: |
Supplemental Index |
Externí odkaz: |
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