Kumar Janesh, Weber Wolfgang, Münchau Sabine, Yadav Savita, Singh S Bhaskar, Saravanan K, Paramasivam M, Sharma Sujata, Kaur Punit, Bhushan A, Srinivasan A, Betzel Christian, Singh T P
Department of Biophysics, All India Institute of Medical Sciences, New Delhi 110029, India.
Indian J Biochem Biophys. 2003 Feb;40(1):14-21.
Lactoferrin was purified from human seminal fluid obtained from the semen bank. The purified samples were saturated with Fe3+ and crystallized by microdialysis method. The crystals belong to orthorhombic space group P21212, with a = 55.9 Angstrom. b = 97.2 Angstrom, c = 156.1 Angstrom and Z = 4. The structure was determined with molecular replacement method and refined to an R factor of 18.7% for all the data to 3.4 Angstrom resolution. The overall structure of seminal lactoferrin is similar to human colostrum lactoferrin. The amino acid sequence of seminal lactoferrin shows that it has one amino acid less than human colostrum lactoferrin and the structure of its N-terminal region is far more ordered than other lactoferrins. The structure of the iron-binding site and its immediate surroundings indicate well defined features.
乳铁蛋白是从精液库获得的人类精液中纯化出来的。纯化后的样品用Fe3+饱和，并通过微透析法结晶。晶体属于正交晶系空间群P21212，a = 55.9埃，b = 97.2埃，c = 156.1埃，Z = 4。采用分子置换法确定了结构，并对所有3.4埃分辨率的数据进行精修，R因子为18.7%。精液乳铁蛋白的整体结构与人类初乳乳铁蛋白相似。精液乳铁蛋白的氨基酸序列表明，它比人类初乳乳铁蛋白少一个氨基酸，并且其N端区域的结构比其他乳铁蛋白更加有序。铁结合位点及其紧邻环境的结构显示出明确的特征。
