Role of DDR2 ECD Oligomerization in Binding to Collagen
Role of DDR2 ECD Oligomerization in Binding to Collagen
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DOI：
10.1017/s1431927616006474
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发表时间：
2016-07
影响因子：
2.8
通讯作者：
Carolyn Wang;D. Yeung;Jack Wellerming;A. Herr;Jeanette L. C. Miller;R. Fridman;G. Agarwal
中科院分区：
文献类型：
--
作者：
Carolyn Wang;D. Yeung;Jack Wellerming;A. Herr;Jeanette L. C. Miller;R. Fridman;G. Agarwal
盘状蛋白结构域受体（DDR1 和 DDR2）是广泛表达的受体酪氨酸激酶 (RTK)，可调节细胞分化、增殖、迁移以及细胞外基质的重塑 [1]。胶原蛋白是唯一已知的 DDR 配体 [2]。近年来，受体的胶原蛋白结合域（图 1）及其在胶原蛋白三螺旋上的结合位点已被阐明 [3]。然而，受体寡聚化在 DDR-胶原蛋白相互作用中的作用尚不完全清楚。这尤其重要，因为受体寡聚化可以调节受体配体结合以及受体磷酸化和激活以及下游信号传导事件。
Discoidin Domain Receptors (DDR1 and DDR2) are widely expressed receptor tyrosine kinases (RTK) that regulate cell differentiation, proliferation and migration and remodeling of the extracellular matrix [1]. Collagen(s) are the only known ligand for DDRs [2]. Both the collagen binding domains of the receptors (Figure 1) as well as their binding site on the collagen triple helix have been elucidated in recent years [3]. However, the role of receptor oligomerization in DDR-collagen interaction is not completely understood. This is especially important as receptor oligomerization can modulate receptorligand binding as well as receptor phosphorylation and activation and downstream-signaling events.