Burgess Antony W, Cho Hyun-Soo, Eigenbrot Charles, Ferguson Kathryn M, Garrett Thomas P J, Leahy Daniel J, Lemmon Mark A, Sliwkowski Mark X, Ward Colin W, Yokoyama Shigeyuki
Cooperative Research Centre for Cellular Growth Factors, P.O. Box 2008, Royal Melbourne Hospital, Parkville, Victoria 3050, Australia.
Mol Cell. 2003 Sep;12(3):541-52. doi: 10.1016/s1097-2765(03)00350-2.
Recent crystallographic studies have provided significant new insight into how receptor tyrosine kinases from the EGF receptor or ErbB family are regulated by their growth factor ligands. EGF receptor dimerization is mediated by a unique dimerization arm, which becomes exposed only after a dramatic domain rearrangement is promoted by growth factor binding. ErbB2, a family member that has no ligand, has its dimerization arm constitutively exposed, and this explains several of its unique properties. We outline a mechanistic view of ErbB receptor homo- and heterodimerization, which suggests new approaches for interfering with these processes when they are implicated in human cancers.
最近的晶体学研究为表皮生长因子（EGF）受体或ErbB家族的受体酪氨酸激酶如何受其生长因子配体调控提供了重要的新见解。EGF受体二聚化由一个独特的二聚化臂介导，该二聚化臂仅在生长因子结合促进显著的结构域重排后才会暴露。ErbB2是该家族中没有配体的成员，其二聚化臂持续暴露，这解释了它的一些独特性质。我们概述了ErbB受体同二聚化和异二聚化的机制观点，这为在这些过程与人类癌症相关时干扰它们提供了新方法。
