cDNA-Derived Amino Acid Sequence from Rat Brain A2aR Possesses Conserved Motifs PMNYM of TM 5 Domain, Which May Be Involved in Dimerization of A2aR
| Autor: | Amresh Prakash, Ramraghubir Ramraghubir, Sandeep Kumar Barodia, Pratibha Mehta Luthra |
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| Rok vydání: | 2007 |
| Předmět: | |
| Zdroj: | Pattern Recognition in Bioinformatics ISBN: 9783540752851 PRIB |
| Popis: | The human adenosine A2a receptor (A2aR) belongs to the family of G-protein coupled receptors (GPCRs), characterized by seven transmembrane (TM) helices. TMs are involved in various cellular processes including dimerization-mediated recognition of ligand. TM5 has been suggested to self associate and may be involved in the dimerization of A2aR. However the role of dimerization and the motifs involved in dimerization of TM 5 have not been revealed. To study the folding and assembly of A2aR, the cDNA of the adenosine A2aR from rat brain was isolated and sequenced (DQ098650). The computational analysis (gi|70727927|gb|AAZ07991.1|) showed that the protein of 42 amino acid residues aligned in TM 5 domain region of AA2AR_RAT (P30543). PROSITE search illustrated that the motif PMNYM was conserved in A2aR and the motif PMSYM was present in A2bR respectively. The minimal dimerization motif in the TM 5 domain of the rat A2a receptor sequence DQ098650 has found to be the motif PXXXM/Y. |
| Databáze: | OpenAIRE |
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