Antithrombin histidine variants 1H NMR resonance assignments and functional properties

FEBS Letters

Fan, Bingqi²  Gettins, Peter G.W.²  Turko, Illarion V.¹ 

[1] Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA;Department of Biochemistry, University of Illinois at Chicago, Chicago, IL 60612, USA

关键词: Antithrombin;    Site-directed mutagenesis;    NMR assignment;    Histidine;    Heparin binding site;   

DOI  :  10.1016/0014-5793(94)01083-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Three variants of the 57.5 kDa human plasma proteinase inhibitor antithrombin, H1Q, H65C, and H120C, have been expressed in baby hamster kidney cells to permit assignment of the ¹H NMR resonances from the three histidines and evaluation of the role of these histidines in heparin binding. The NMR assignments have enabled more definitive interpretation of previous NMR-based studies of human antithrombin to be made. Although resonances of all three histidines are perturbed by heparin binding, only histidine 120 plays a significant role in the heparin binding site. The perturbations of resonances from histidines 1 and 65 indicate proximity to the heparin binding site and consequent sensitivity to the presence of heparin.

【 授权许可】

Unknown