Kamata T, Takada Y
Department of Vascular Biology, Scripps Research Institute, La Jolla, California 92037.
J Biol Chem. 1994 Oct 21;269(42):26006-10.
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.
整合素α2β1是一种主要的依赖二价阳离子的胶原蛋白受体。在此，我们表明α2的重组插入/相互作用结构域（I结构域）特异性地与胶原蛋白相互作用，这表明I结构域包含胶原蛋白结合所需的所有成分。有证据表明，二价阳离子对于胶原蛋白与I结构域片段的结合并非必需，这表明二价阳离子不参与与胶原蛋白的实际结合，但可能参与结合的调节。我们确定了先前鉴定的假定配体结合区域内的苏氨酸-221是胶原蛋白与α2β1和I结构域片段结合的关键残基。苏氨酸-221可能参与了与胶原蛋白的实际结合和识别。
