The 1.1 Å crystal structure of human TGF-β type II receptor ligand binding domain
The 1.1 Å crystal structure of human TGF-β type II receptor ligand binding domain
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DOI：
10.1016/s0969-2126(02)00780-3
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发表时间：
2002-07-01
期刊：
影响因子：
5.7
通讯作者：
Sun, PD
中科院分区：
文献类型：
--
作者：
Boesen, CC;Radaev, S;Sun, PD
转化生长因子β（TGF-β）参与广泛的生物学功能，包括发育、致癌和免疫调节。在这里，我们报告的1.1埃分辨率的晶体结构的人TGF-β II型受体胞外域（TBRII）。TBRII的整体结构与激活素II型受体胞外域（ActRII）和骨形态发生蛋白受体IA型（BRIA）的结构相似。它展示了一个三指毒素折叠，其中指由β链对β 1-β 2、β 3-β 4和β 5-β 6形成。TBRII中的第一指明显长于ActRII和BRIA中的第一指，并且在第二指和C末端之间紧密折叠。表面电荷分布和疏水补丁预测潜在的TBRII结合位点。
Transforming growth factor beta (TGF-beta) is involved in a wide range of biological functions including development, carcinogenesis, and immune regulation. Here we report the 1.1 Angstrom resolution crystal structure of human TGF-beta type II receptor ectodomain (TBRII). The overall structure of TBRII is similar to that of activin type II receptor ectodomain (ActRII) and bone morphogenic protein receptor type IA (BRIA). It displays a three-finger toxin fold with fingers formed by the beta strand pairs beta1-beta2, beta3-beta4, and beta5-beta6. The first finger in the TBRII is significantly longer than in ActRII and BRIA and folds tightly between the second finger and the C terminus. Surface charge distributions and hydrophobic patches predict potential TBRII binding sites.