牛血清白蛋白
血清白蛋白
化学
白蛋白
结构相似性
配体(生物化学)
结合位点
高分子
生物化学
受体
作者
B. Sekula,Kamil Zielinski,A. Bujacz
标识
DOI:10.1016/j.ijbiomac.2013.06.004
摘要
Due to their extraordinary binding properties, serum albumins are the main transporters of many small molecules in the circulatory system. Although all mammalian serum albumins exhibit quite high sequence similarity, their binding abilities are not the same. Until now, only human serum albumin (HSA) was subjected to extensive structural studies in complexes with various ligands. Here we present two crystal structures of the complexes of equine and bovine serum albumins with 3,5-diiodosalicylic acid (DIS), at resolutions 2.12 Å and 2.65 Å, respectively, and analyze interactions of the DIS ligand with both macromolecules. We highlight the differences in distribution of DIS binding sites between the bovine and equine serum albumins and compare results with the HSA binding ability of DIS and other structurally similar ligands.
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