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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
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- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제14권 제5호
- 발행연도
- 2004.1
- 수록면
- 1,031 - 1,037 (7page)
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The interaction of chemoattractant receptors andGα16 was studied to provide the molecular basis to elucidatethe interaction of chemoattractant receptors with Gα16 subunit,thereby possibly contributing to finding novel targets for designingnew type of G protein antagonists with anti-inflammatoryeffects. Experiments were performed to characterize theGα16 subunit domains responsible for efficient coupling tochemoattractant receptors. Thus, a series of chimeric Gα11/Gα16and Gα16/Gα11 cDNA constructs were expressed, and the abilityof chimeric proteins to mediate C5a, IL-8, and fMLP-inducedrelease of inositol phosphate in transfected Cos-7 cells wastested. The results showed that short stretches of residues 154 toresidue 167 and from residue 174 to residue 195 of Gα16contribute to efficient coupling to the C5a receptor. On the otherhand, a stretch of amino acid residues 220- 240 of Gα16 that isnecessary for interacting with C5a receptor did not play any rolein the interaction with IL-8 receptor. However, a stretch fromresidue 155 to residue 195 of Gα16 was found to be crucial forefficient coupling to IL-8 receptor in concert with C-terminal 30amino acid residues of this α subunit. Coupling profiles of avariety of chimeras, composed of Gα11 and Gα16, to fMLPreceptor indicate that the C-terminal 30 amino acids are mostcritical for the coupling of Gα16 to fMLP receptor. Takentogether, Gα16 subunit recruits multiple and distinctive couplingregions, depending on the type of receptors, to interact.
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참고문헌 (28)
참고문헌 신청
[학
A / 1991 / a G protein α subunit specificallyexpressed in hematopoietic cells : 5587 ~ 5591
A / 1993 / NMR structure of a receptor-bound G-protein peptide : 276 ~ 363 281
Amatruda, 3rd T. T / 1995 / Signal transduction by the formyl peptidereceptor Studies using chimeric receptors and site-directedmutagenesis define a novel domain for interact
Beckmann / 1991 / Molecular characterization of the interleukin-8 receptor : 784 ~ 789
A / 1991 / a G protein α subunit specificallyexpressed in hematopoietic cells : 5587 ~ 5591
A / 1993 / NMR structure of a receptor-bound G-protein peptide : 276 ~ 363 281
Amatruda, 3rd T. T / 1995 / Signal transduction by the formyl peptidereceptor Studies using chimeric receptors and site-directedmutagenesis define a novel domain for interact
Beckmann / 1991 / Molecular characterization of the interleukin-8 receptor : 784 ~ 789
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