Maurer P, Hohenester E, Engel J
Institute for Biochemistry, Medical Faculty, University of Köln, Joseph-Stelzmann-Strasse 52, 50931 Köln, Germany.
Curr Opin Cell Biol. 1996 Oct;8(5):609-17. doi: 10.1016/s0955-0674(96)80101-3.
Point mutations in Ca2+-binding sites of extracellular matrix proteins have been identified as the cause of human disorders such as Marfansyndrome and pseudoachondroplasia. Although the modes of Ca2+ binding and the effects of point mutations are not yet understood in these two cases, new insight was recently gained by X-ray and NMR structure determinations of several other extracellular proteins; these studies revealed a diversity of functions of Ca2+ ions. Ca2+ may induce a profound conformational change within a single domain, may bridge adjacent domains and thus direct the relative domain orientation and supramolecular structure, or may be involved in carbohydrate and membrane binding.
细胞外基质蛋白钙离子结合位点的点突变已被确认为诸如马凡综合征和假性软骨发育不全等人类疾病的病因。尽管在这两种情况下钙离子的结合模式和点突变的影响尚不清楚，但最近通过对其他几种细胞外蛋白的X射线和核磁共振结构测定获得了新的见解；这些研究揭示了钙离子的多种功能。钙离子可能在单个结构域内诱导深刻的构象变化，可能连接相邻结构域从而指导相对结构域取向和超分子结构，或者可能参与碳水化合物和膜的结合。
