Grossmann J G, Neu M, Evans R W, Lindley P F, Appel H, Hasnain S S
Molecular Biophysics Group, SERC Daresbury Laboratory, Warrington, Cheshire, U.K.
J Mol Biol. 1993 Feb 5;229(3):585-90. doi: 10.1006/jmbi.1993.1063.
Recent studies on iron-loaded transferrins have revealed a conformational change upon binding iron due to a domain closure. It has been suggested that the domain closure may be the key for the receptor recognition of the metal loaded transferrin (Grossmann et al., 1992). Small angle X-ray scattering has been used to provide direct structural information on the conformational changes that may take place upon the binding and release of different metals to the transferrins in solution. The data show that In3+ and Cu2+ induce the same domain closure as Fe3+; Al3+ causes a conformational change of somewhat smaller magnitude while Hf4+ does not induce any conformational change. The results are discussed in terms of the molecular recognition of metal loaded transferrin by the receptor.
最近对铁负载转铁蛋白的研究表明,由于结构域闭合,铁结合后会发生构象变化。有人提出,结构域闭合可能是受体识别金属负载转铁蛋白的关键(格罗斯曼等人,1992年)。小角X射线散射已被用于提供有关不同金属在溶液中与转铁蛋白结合和释放时可能发生的构象变化的直接结构信息。数据表明,In3+和Cu2+诱导的结构域闭合与Fe3+相同;Al3+引起的构象变化幅度稍小,而Hf4+不诱导任何构象变化。根据受体对金属负载转铁蛋白的分子识别对结果进行了讨论。