Kohfeldt E, Maurer P, Vannahme C, Timpl R
Max-Planck-Institut für Biochemie, Martinsried, Germany.
FEBS Lett. 1997 Sep 15;414(3):557-61. doi: 10.1016/s0014-5793(97)01070-3.
The extracellular calcium-binding (EC) module of human testican (115 residues) was obtained in native form by recombinant production in mammalian cell culture and thus shown to represent an independently folding domain. This module showed a large loss in alpha-helix upon calcium depletion. Apparently only one of the two EF hands binds calcium, with a moderate affinity (Kd =68 microM) about 100-fold lower than in the homologous BM-40 protein. No clear evidence was obtained for collagen binding, indicating that EC modules found in different proteins may not share similar functions.
人睾丸蛋白聚糖的细胞外钙结合(EC)模块(115个氨基酸残基)通过在哺乳动物细胞培养中重组生产以天然形式获得,因此显示为一个独立折叠的结构域。该模块在钙耗尽时α螺旋大量丢失。显然,两个EF手型结构中只有一个结合钙,亲和力适中(Kd = 68 μM),比同源的BM - 40蛋白低约100倍。未获得与胶原蛋白结合的明确证据,表明在不同蛋白质中发现的EC模块可能不具有相似功能。