1DM4

SER195ALA MUTANT OF HUMAN THROMBIN COMPLEXED WITH FIBRINOPEPTIDE A (7-16)

1DM4 の概要

• エントリーDOI: 10.2210/pdb1dm4/pdb
• 分子名称: PROTEIN (ALPHA THROMBIN:LIGHT CHAIN), PROTEIN (MUTANT ALPHA THROMBIN:HEAVY CHAIN), PROTEIN (FIBRINOPEPTIDE), ... (4 entities in total)
• 機能のキーワード: mutant thrombin, residual catalytic activity, fibrinopeptide a, hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Secreted, extracellular space: P00734 P00734
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 34907.90

構造登録者

Krishnan, R.,Sadler, E.J.,Tulinsky, A. (登録日: 1999-12-13, 公開日: 2000-01-19, 最終更新日: 2024-10-16)

主引用文献

Krishnan, R.,Sadler, J.E.,Tulinsky, A.
Structure of the Ser195Ala mutant of human alpha--thrombin complexed with fibrinopeptide A(7--16): evidence for residual catalytic activity.
Acta Crystallogr.,Sect.D, 56:406-410, 2000

PubMed Abstract: The Ser195Ala mutant of human alpha-thrombin was complexed with fibrinopeptide A(7-22) (FPA) in an effort to describe the (P1'-P6') post-cleavage binding subsites of the fibrinogen-recognition exosite and define more clearly the nature of the Michaelis complex and the scissile peptide bond bound at the catalytic site. The thrombin mutant, however, has residual catalytic activity and proteolysis occurred at the Arg16-Gly17 bond. Thus, the structure of the thrombin complex determined was that of FPA(7-16) bound at the active site, which is very similar to the ternary FPA(7-16)cmk-human thrombin-hirugen complex (r.m.s.d. approximately 0.4 A; Stubbs et al. , 1992). It is further shown by subsidiary experiments that the cleavage is the result of residual catalytic activity of the altered catalytic machinery.

PubMed: 10739913
DOI: 10.1107/S0907444900001487

実験手法

X-RAY DIFFRACTION (2.5 Å)