Calcium-induced environmental adaptability of the blood protein vitronectin. Biophys J 2022 Oct 18;121(20):3896-3906
Date
09/04/2022Pubmed ID
36056555Pubmed Central ID
PMC9674982DOI
10.1016/j.bpj.2022.08.044Scopus ID
2-s2.0-85137693880 (requires institutional sign-in at Scopus site) 2 CitationsAbstract
The adaptability of proteins to their work environments is fundamental for cellular life. Here, we describe how the hemopexin-like domain of the multifunctional blood glycoprotein vitronectin binds Ca2+ to adapt to excursions of temperature and shear stress. Using X-ray crystallography, molecular dynamics simulations, NMR, and differential scanning fluorimetry, we describe how Ca2+ and its flexible hydration shell enable the protein to perform conformational changes that relay beyond the calcium-binding site and alter the number of polar contacts to enhance conformational stability. By means of mutagenesis, we identify key residues that cooperate with Ca2+ to promote protein stability, and we show that calcium association confers protection against shear stress, a property that is advantageous for proteins that circulate in the vasculature, like vitronectin.
Author List
Tian Y, Shin K, Aleshin AE, Im W, Marassi FMAuthors
Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of WisconsinKyungsoo Shin PhD Assistant Professor in the Biophysics department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
Binding SitesCalcium
Crystallography, X-Ray
Hemopexin
Protein Binding
Protein Conformation
Vitronectin
