1KIG

BOVINE FACTOR XA

1KIG の概要

• エントリーDOI: 10.2210/pdb1kig/pdb
• 分子名称: FACTOR XA, ANTICOAGULANT PEPTIDE (3 entities in total)
• 機能のキーワード: glycoprotein, serine protease, plasma, blood coagulation, complex (protease-inhibitor), complex (protease-inhibitor) complex, complex (protease/inhibitor)
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Secreted: P00743 P00743
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 39473.39

構造登録者

Wei, A.,Alexander, R.,Chang, C.-H. (登録日: 1997-04-24, 公開日: 1998-10-28, 最終更新日: 2024-10-23)

主引用文献

Wei, A.,Alexander, R.S.,Duke, J.,Ross, H.,Rosenfeld, S.A.,Chang, C.H.
Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa.
J.Mol.Biol., 283:147-154, 1998

PubMed Abstract: The structure of recombinant tick anticoagulant peptide (rTAP) complexed to bovine factor Xa at 3.0 A resolution reveals the structural basis for the specificity and the high affinity of rTAP. Three N-terminal residues, Tyr501, Asn502 and Arg503, play a critical role in the complex formation as suggested by earlier mutagenic studies and the ornithodorin-thrombin complex. Unexpectedly, the side-chain of Tyr501 is located in the S1 pocket, although factor Xa favors arginine as a P1 residue. Arg503 is located at the aryl binding pocket and forms a salt-bridge with Glu97 of factor Xa. The autolysis loop, which is disordered in the uninhibited factor Xa structure, is involved in the formation of the complex as a part of the secondary binding site. The C-terminal helix of rTAP interacts with factor Xa as a secondary binding determinant. The N-terminal residues of rTAP reorganize during the formation of the factor Xa-rTAP complex from the conformation found in the solution into an extended conformation. The presence of the secondary binding site confirms the proposed two-step kinetic mechanism based on the results of a mutagenesis study.

PubMed: 9761680
DOI: 10.1006/jmbi.1998.2069

実験手法

X-RAY DIFFRACTION (3 Å)