A low resolution model of fragment 1 from bovine prothrombin
نویسندگان
چکیده
منابع مشابه
The effect of divalent metal ions on the electrophoretic mobility of bovine prothrombin and bovine prothrombin fragment 1.
Examination of metal ion-dependent effects on the electrophoretic mobility of bovine prothrombin and fragment 1 provides a useful and sensitive method for investigation of conformational processes in these proteins. Utilization of this method reveals a conformational change in bovine prothrombin and fragment 1 which occurs at low metal ion concentrations. Equilibrium dialysis studies indicate t...
متن کاملSolution conformations of the gamma-carboxyglutamic acid domain of bovine prothrombin fragment 1, residues 1-65.
Molecular dynamics simulations have been performed (AMBER version 3.1) on solvated residues 1-65 of bovine prothrombin fragment 1 (BF1) by using the 2.8-A resolution crystallographic coordinates as the starting conformation for understanding calcium ion-induced conformational changes that precede experimentally observable phospholipid binding. Simulations were performed on the non-metal-bound c...
متن کاملTrans-cis isomerization of proline 22 in bovine prothrombin fragment 1: a surprising result of structural characterization.
The calcium ion-mediated interaction of bovine prothrombin (BF1) with negatively charged phospholipid membranes is assumed to be largely via the Gla domain of BF1 with the fold of the Gla domain essential for binding. It has been reported that Pro22 undergoes classical trans to cis isomerization in the presence of calcium ions with the cis conformation of Pro22 of BF1 responsible for membrane b...
متن کاملLeft atrial thrombin generation and prothrombin fragment 1+2.
Peverill and colleagues [1] recently reported differences in levels of prothrombin fragment 12 (F12) in blood obtained from the left atrium, the femoral artery and the femoral vein from 36 patients with mitral stenosis. They aimed (i) to compare arterial and venous levels of F12 in patients with normal clotting times, (ii) to examine and compare the relationship between arterial and venous l...
متن کاملPhospholipid binding properties of bovine prothrombin peptide residues 1-45.
The present study investigates the unique contribution of the NH2-terminal 33 residues of prothrombin, the gamma-carboxyglutamic acid (Gla) domain, to the Ca(II) and phospholipid-binding properties of prothrombin. Two Gla domain peptides, 1-42 and 1-45, produced by chymotryptic cleavage of prothrombin fragment 1 (residues 1-156 of the amino terminus of bovine prothrombin) and isolated by anion-...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1982
ISSN: 0014-5793
DOI: 10.1016/0014-5793(82)80191-9