期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 60, 期 -, 页码 316-324出版社
ELSEVIER
DOI: 10.1016/j.ijbiomac.2013.06.004
关键词
Crystal structure; Bovine and equine serum albumins; 3,5-Diiodosalicylic acid binding sites
资金
- Polish Ministry of Science and Higher Education [N N405 3639 39]
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 angstrom and 2.65 angstrom, 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. (C) 2013 Elsevier B.V. All rights reserved.
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