Role of tryptophan 49 in the heparin cofactor activity of human antithrombin III

• Published in: The Journal of biological chemistry Vol. 267; no. 30; pp. 21946 - 21953
• Main Authors: Gettins, P, Choay, J, Crews, B.C., Zettlmeiss, G
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 25.10.1992; American Society for Biochemistry and Molecular Biology
• Subjects: activity; Analytical, structural and metabolic biochemistry; Animals; antithrombin III; Antithrombin III - genetics; Antithrombin III - isolation & purification; Antithrombin III - metabolism; Biological and medical sciences; Cells, Cultured; cofactors; Cricetinae; Electrophoresis, Polyacrylamide Gel; Fluorescence; Fundamental and applied biological sciences. Psychology; Glycoproteins; heparin; Heparin - metabolism; Humans; Magnetic Resonance Spectroscopy; man; Mutation; Proteins; Recombinant Proteins - isolation & purification; Recombinant Proteins - metabolism; role; Substrate Specificity; tryptophan; Tryptophan - genetics; Tryptophan - metabolism; Human; Ligand binding; Structure activity relation; Antithrombin III; Tryptophan; NMR spectrometry; Heparin; Fluorescence spectrometry

To probe the functional role of tryptophan 49 in human antithrombin III, a mutant antithrombin, W49K, has been expressed in baby hamster kidney cells. The mutation reduces the affinity for heparin pentasaccharide by 1.8 kcal mol-1 but does not alter the heparin enhancement of the rate of factor Xa i...