1APO

THREE-DIMENSIONAL STRUCTURE OF THE APO FORM OF THE N-TERMINAL EGF-LIKE MODULE OF BLOOD COAGULATION FACTOR X AS DETERMINED BY NMR SPECTROSCOPY AND SIMULATED FOLDING

1APO の概要

• エントリーDOI: 10.2210/pdb1apo/pdb
• 分子名称: EGF-LIKE MODULE OF BLOOD COAGULATION FACTOR X, HYDROXIDE ION (2 entities in total)
• 機能のキーワード: coagulation factor
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Secreted: P00743
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4577.96

構造登録者

Ullner, M.,Selander, M.,Persson, E.,Stenflo, J.,Drakenberg, T.,Teleman, O. (登録日: 1992-04-21, 公開日: 1994-01-31, 最終更新日: 2025-03-26)

主引用文献

Ullner, M.,Selander, M.,Persson, E.,Stenflo, J.,Drakenberg, T.,Teleman, O.
Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding.
Biochemistry, 31:5974-5983, 1992

PubMed Abstract: The three-dimensional structure of a 42-residue fragment containing the N-terminal EGF-like module of blood coagulation factor X was determined by means of 2D NMR spectroscopy and computer simulation. The spectroscopic data consisted of 370 NOE distances and 27 dihedral angle constraints. These were used to generate peptide conformations by molecular dynamics simulation. The simulations used a novel functional form for the constraint potentials and were performed with two time steps to ensure rapid execution. Apart from preliminary runs to aid assignment of NOEs, 60 runs resulted in 13 accepted structures, which have two antiparallel beta sheets, no alpha helices, and five tight turns. There is no hydrophobic cluster. The root mean square deviation for the backbone of the 13 conformations is 0.65 +/- 0.11 A against their mean conformation. About half of the side chains have well-defined structure. The overall conformation is similar to that of murine EGF.

PubMed: 1627540
DOI: 10.1021/bi00141a004

実験手法

SOLUTION NMR