The dual role of CHAPS in the crystallization of stromelysin-3 catalytic domain
The dual role of CHAPS in the crystallization of stromelysin-3 catalytic domain
复制标题
DOI：
10.1107/s0907444902017870
复制
发表时间：
2003-03-01
期刊：
影响因子：
--
通讯作者：
Moras, D
中科院分区：
文献类型：
--
作者：
Gall, AL;Ruff, M;Moras, D
CHAPS {3-[(3-胆酰胺丙基)二甲基铵]-1-丙烷磺酸}是一种非变性洗涤剂，广泛用于蛋白质溶解和稳定。 CHAPS 用于避免重组 Stromelysin-3 (ST3) 催化结构域浓缩期间蛋白质聚集，并需要稳定蛋白质，使其结晶。 ST3 催化结构域和次膦酸抑制剂之间的复合物的晶体结构显示两个 CHAPS 分子以两个不同的方向与 ST3 结合。一个 CHAPS 分子掩盖了蛋白质的疏水表面，从而避免了蛋白质聚集。这种去污剂分子也参与堆积相互作用。另一个去垢剂分子位于 ST3 N 端和 C 端部分形成的口袋中，并稳定通常结合 Ca 原子的环。
CHAPS {3-[(3-cholamidopropyl) dimethylammonio]-1-propane sulfonate} is a non-denaturing detergent widely used for protein solubilization and stabilization. CHAPS was used to avoid protein aggregation during concentration of the recombinant stromelysin-3 (ST3) catalytic domain and was required to stabilize the protein, allowing its crystallization. The crystal structure of the complex between the ST3 catalytic domain and a phosphinic inhibitor shows two CHAPS molecules binding to ST3 in two different orientations. One CHAPS molecule is masking a hydrophobic surface of the protein, thus avoiding protein aggregation. This detergent molecule is also involved in packing interactions. The other detergent molecule is located in a pocket formed by the N- and C-terminal parts of the ST3 and stabilizes a loop that normally binds a Ca atom.