X-ray structural analysis of bovine lactoferrin at 2.5 A resolution.

X-ray structural analysis of bovine lactoferrin at 2.5 A resolution.
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牛乳铁蛋白的 X 射线结构分析,分辨率为 2.5 A。

DOI:
10.1007/978-1-4615-2548-6_24
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发表时间:
1994
影响因子:
--
通讯作者:
Baker,EN
Baker,EN
中科院分区:
医学4区
文献类型:
--
作者:
Haridas,M;Anderson,BF;Baker,HM;Norris,GE;Baker,EN

文献摘要

被引文献

相似文献

虽然已经用高分辨率的X射线结晶学分析(Bakeret al,本卷)确定了不同功能状态下的人乳铁蛋白的三维结构,但仍有充分的理由研究其他物种的乳铁蛋白的结构。物种之间发生的序列差异会导致性质上的细微变化,并为更密切地分析结构和功能之间的关系提供了机会。此外,关于人类乳铁蛋白的结构工作已经确定了各种灵活性元素(Bakeret al,1991),这些元素可以在物种变异中表现出来。
Although the three-dimensional structure of human lactoferrin, in various functional states, has been determined by X-ray crystallographic analysis at high resolution (Bakeret al, this volume) there are good reasons to investigate the structures of lactoferrins of other species. The sequence variations which occur between species result in subtle changes in properties and offer the opportunity to more closely analyse the relationships between structure and function. Moreover the structural work on human lactoferrin has identified various elements of flexibility (Bakeret al, 1991), which could be expressed in species variations.