ON THE TERTIARY STRUCTURE OF THE EXTRACELLULAR DOMAINS OF THE EPIDERMAL GROWTH-FACTOR AND INSULIN-RECEPTORS
ON THE TERTIARY STRUCTURE OF THE EXTRACELLULAR DOMAINS OF THE EPIDERMAL GROWTH-FACTOR AND INSULIN-RECEPTORS
复制标题
DOI：
10.1016/0167-4838(87)90112-9
复制
发表时间：
1987-11-26
期刊：
影响因子：
--
通讯作者：
BLUNDELL, T
中科院分区：
文献类型：
--
作者：
BAJAJ, M;WATERFIELD, MD;BLUNDELL, T
序列比对、保守残基模式的鉴定和二级结构预测表明，人和果蝇表皮生长因子、c-erb-B2和人胰岛素受体的胞外区域都包含两个大的同源结构域(L)，这两个结构域可能至少由四个短的α-螺旋组成，然后是保守长度和β-链的交替。在人和果蝇的EGF和c-erb-B2受体中，这些同源结构域后面都有一系列较小的胱氨酸富集区(S)，从而形成了L1S11S12S13L2 S21S22S23的基因复制结构。在人类胰岛素受体中，第二系列半胱氨酸区被不同的序列所取代。这些重复的结构很可能是以伪对称二聚体的形式组织的。有两个‘’高变区‘’，一个在大的优势末端，一个在富含半胱氨酸的序列中，它们是激素或生长因子结合的候选者。
Alignment of the sequences, the identification of conserved residue patterns and secondary structure predictions indicate that the extra-cellular regions of the human and Drosophila epidermal growth factor (EGF), c-erb-B2 and human insulin receptor each contain two large, homologous domains (L) which are probably comprised of at least four short .alpha.-helices followed by turns of conserved length and .beta.-strands. In the human and Drosophila EGF and c-erb-B2 receptors these homologous domains are each followed by a series of smaller cystine-rich domains (S) to give a gene-duplicated structure of L1S11S12S13L2 S21S22S23. In the human insulin receptor, the second series of cystine domains is replaced by a different sequence. These duplicated structures are probably organised as a pseudo-symmetrical dimer. There are two ''hypervariable'' regions, one at the end of the large dominas and one in the cystine-rich sequences, which are candidates for hormone or growth-factor binding.