Direct binding of collagen to the I domain of integrin alpha 2 beta 1 (VLA-2, CD49b/CD29) in a divalent cation-independent manner.
Direct binding of collagen to the I domain of integrin alpha 2 beta 1 (VLA-2, CD49b/CD29) in a divalent cation-independent manner.
复制标题
DOI：
10.1016/s0021-9258(18)47151-7
复制
发表时间：
1994-10
期刊：
影响因子：
--
通讯作者：
T. Kamata;Yoshikazu Takada
中科院分区：
文献类型：
--
作者：
T. Kamata;Yoshikazu Takada
整合素α2β1是一种主要的二价阳离子依赖的胶原受体。在这里，我们证明了α2的重组插入/相互作用结构域(I结构域)与胶原特异地相互作用，表明I结构域包含胶原结合所需的所有成分。有证据表明，二价阳离子不是胶原与I结构域片段结合所必需的，这表明二价阳离子并不参与与胶原的实际结合，但可能参与了结合的调节。我们在先前确定的配体结合区中确定Thr-221是胶原蛋白与α2β1和I结构域片段结合的关键残基。Thr-221可能参与了胶原蛋白的结合和识别。
Integrin alpha 2 beta 1 is a major divalent cation-dependent receptor for collagen. Here, we show that the recombinant inserted/interactive domain (I domain) of alpha 2 specifically interacts with collagen, indicating the I domain contains all the components necessary for collagen binding. Evidence was obtained that divalent cations are not required for collagen binding to the I domain fragment, indicating that divalent cations are not involved in the actual binding to collagen but probably in the regulation of the binding. We identified Thr-221 within the previously identified putative ligand binding region as a residue critical for collagen binding to both alpha 2 beta 1 and the I domain fragment. Thr-221 may be involved in the actual collagen binding and recognition.