Max-Planck Institute for Experimental Medicine, Department of Molecular Neuroendocrinology, Hermann-Rein-Strasse 3, 37075 Goettingen, Germany.
Trends Endocrinol Metab. 1998 May-Jun;9(4):140-5. doi: 10.1016/s1043-2760(98)00037-x.
Research into the biology of corticotropin-releasing factor (CRF) has been intensified significantly by the structural characterization of the CRF receptor (CRF-R). Two receptor subtypes, CRF-R1 and CRF-R2, and three functional splice variants of CRF-R2 have been discovered. It appears that ligand binding requires interaction of the N-terminal domain with one or two other extracellular domains of the CRF-R. In contrast to the mammalian CRF-R1, the frog CRF-R1 discriminates between naturally occurring CRF-like peptides.
对促肾上腺皮质释放因子(CRF)生物学的研究因 CRF 受体(CRF-R)的结构特征而显著加强。已经发现了两种受体亚型,CRF-R1 和 CRF-R2,以及 CRF-R2 的三个功能剪接变体。似乎配体结合需要 N 端结构域与 CRF-R 的一个或两个其他细胞外结构域相互作用。与哺乳动物的 CRF-R1 不同,蛙类的 CRF-R1 可区分天然存在的 CRF 样肽。