Crystal structures of serum albumins from domesticated ruminants and their complexes with 3,5-diiodosalicylic acid.

ABSTRACT: Serum albumin (SA) is the most abundant protein in plasma and is the main transporter of molecules in the circulatory system of all vertebrates, with applications in medicine, the pharmaceutical industry and molecular biology. It is known that albumins from different organisms vary in sequence; thus, it is important to know the impact of the amino-acid sequence on the three-dimensional structure and ligand-binding properties. Here, crystal structures of ovine (OSA) and caprine (CSA) serum albumins, isolated from sheep and goat blood, are described, as well those of their complexes with 3,5-diiodosalicylic acid (DIS): OSA-DIS (2.20 Å resolution) and CSA-DIS (1.78 Å resolution). The ligand-free OSA structure was determined in the trigonal space group P3₂21 at 2.30 Å resolution, wh

SUBMITTER: Bujacz A 

PROVIDER: S-EPMC5683013 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature