Chapman B S
Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco 94143-0446, USA.
FEBS Lett. 1995 Oct 30;374(2):216-20. doi: 10.1016/0014-5793(95)01113-s.
Members of the NTR/TNFR family mediate apoptosis in many tissues, yet sequence homology has not been detected in their intracellular domains except for a 'death domain' in TNFR-I and Fas. Here, a region of the 75 kDa neurotrophin receptor (NTR) has been aligned with this apoptosis-inducing motif. Peptides at the carboxyl terminus of each domain potentially form amphiphilic helices, one of which (in NTR) resembles mastoparan, a G-protein activating peptide. Molecular models of three death-region peptides suggest that observed sequence similarities reflect a common structure, perhaps capable of undergoing an induced coil to helix transition.
神经营养因子受体/肿瘤坏死因子受体(NTR/TNFR)家族成员在许多组织中介导细胞凋亡,然而,除了肿瘤坏死因子受体-I(TNFR-I)和Fas中的“死亡结构域”外,在它们的细胞内结构域中尚未检测到序列同源性。在此,已将75 kDa神经营养因子受体(NTR)的一个区域与这种诱导细胞凋亡的基序进行了比对。每个结构域羧基末端的肽可能形成两亲性螺旋,其中一个(在NTR中)类似于马斯托帕兰,一种G蛋白激活肽。三种死亡区域肽的分子模型表明,观察到的序列相似性反映了一种共同的结构,或许能够经历诱导的卷曲到螺旋的转变。