Favier-Perron B, Lewit-Bentley A, Russo-Marie F
ICGM, U332 INSERM, Paris, France.
Biochemistry. 1996 Feb 13;35(6):1740-4. doi: 10.1021/bi952092o.
The structure of recombinant human annexin III was solved to 1.8 A resolution. Though homologous to annexin I and V, the annexin III structure shows significant differences. The tryptophan in the calcium loop of the third domain is exposed to the solvent, as in the structure of annexin V crystallized in high calcium concentrations, although the annexin III crystals were prepared at low calcium concentrations. The position of domain III relative to the other domains is different from both annexin V and I, suggesting further flexibility of the molecule. The entire N-terminus of the protein is well-defined in the present structure. The side chain of tryptophan 5 interacts with the hinge region of the hydrophillic channel, which could have an effect on the potential mobility of this region, as well as on its possible calcium channel behavior.
重组人膜联蛋白III的结构解析达到了1.8埃的分辨率。尽管与膜联蛋白I和V同源，但膜联蛋白III的结构显示出显著差异。第三个结构域钙环中的色氨酸暴露于溶剂中，这与在高钙浓度下结晶的膜联蛋白V的结构相同，尽管膜联蛋白III晶体是在低钙浓度下制备的。结构域III相对于其他结构域的位置与膜联蛋白V和I都不同，这表明该分子具有更大的灵活性。在当前结构中，蛋白质的整个N端都定义明确。色氨酸5的侧链与亲水通道的铰链区相互作用，这可能会影响该区域的潜在流动性及其可能的钙通道行为。
