残留21 - 30 C5a受体的细胞外的氨基端区域内代表ca5过敏毒素可以绑定域名。
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陈Z,张X, Gonnella数控,斗篷TC, Boyar WC,倪F
残留21 - 30 C5a受体的细胞外的氨基端区域内代表ca5过敏毒素可以绑定域名。
J生物化学杂志。1998年4月24日,273 (17):10411 - 9。
- PubMed ID
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9553099 (在PubMed]
- 文摘
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ca5的过敏毒素的功能表达通过与细胞表面受体的互动与七个跨膜螺旋。C5a与受体的相互作用解释了two-site模型,识别和效应器C5a绑定网站,分别识别和效应器域受体,受体激活(整个浴盆,d E。Hugli, t . e .(1980)摩尔。Immunol。17岁,151 - 161。此外,细胞外的氨基端区域C5a受体已涉及作为C5a识别域,负责大约50%的结合能C5a-receptor复杂(Mery, L。布雷,f(1994)生物。化学。269年,3457 - 3463;DeMartino, j . A。范成熟,G。西西里岛舞蹈,s . J。,Molineaux曾经c J。Konteatis, z D。罗森,H。施普林格,m . s .(1994)生物。269年化学,14446 - 14450)。在这部作品中,交互的C5a ca5的n端结构域受体检测利用重组人类C5a分子和肽片段M1NSFN5YTTPD10YGHYD15DKDTL20DLNTP25VDKTS30NTLR (hC5aRF-1-34) acetyl-HYD15DKDTL20DLNTP25VDKTS30NTLR (hC5aRF-13-34)和acetyl-TL20DLNTP25VDKTS30N-amide (hC5aRF-19-31)源自人类ca5的受体。绑定诱导共振扰动的核磁共振光谱受体片段和C5a分子表明,孤立Nterminal域或残留的猴C5a保留特定受体结合C5a和C5a模拟缺乏完整C5a争胜c端尾。 Residues of C5a perturbed by the binding of the receptor peptides are localized within the helical core of the C5a structure, in agreement with the results from functional studies employing mutated C5a and intact receptor molecules. All three receptor peptides, hC5aRF-1-34, hC5aRF-13-34, and hC5aRF-19-31, responded to the binding of C5a through the 21-30 region containing either hydrophobic, polar, or positively charged residues such as Thr24, Pro25, Val26, Lys28, Thr29, and Ser30. The 21-30 segment of all three receptor fragments was found to have a partially folded conformation in solution, independent of residues 1-18. These results indicate that a short peptide sequence, or residues 21-30, of the C5a receptor N terminus may constitute the binding domain for the recognition site on C5a.