1FZG

CRYSTAL STRUCTURE OF FRAGMENT D FROM HUMAN FIBRINOGEN WITH THE PEPTIDE LIGAND GLY-HIS-ARG-PRO-AMIDE

1FZG の概要

• エントリーDOI: 10.2210/pdb1fzg/pdb
• 分子名称: FIBRINOGEN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (7 entities in total)
• 機能のキーワード: blood coagulation, plasma, platelet, fibrinogen, fibrin
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 171359.99

構造登録者

Everse, S.J.,Spraggon, G.,Veerapandian, L.,Doolittle, R.F. (登録日: 1999-01-01, 公開日: 1999-06-08, 最終更新日: 2024-10-30)

主引用文献

Everse, S.J.,Spraggon, G.,Veerapandian, L.,Doolittle, R.F.
Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide.
Biochemistry, 38:2941-2946, 1999

PubMed Abstract: The structure of fragment double-D from human fibrin has been solved in the presence and absence of the peptide ligands that simulate the two knobs exposed by the removal of fibrinopeptides A and B, respectively. All told, six crystal structures have been determined, three of which are reported here for the first time: namely, fragments D and double-D with the peptide GHRPam alone and double-D in the absence of any peptide ligand. Comparison of the structures has revealed a series of conformational changes that are brought about by the various knob-hole interactions. Of greatest interest is a moveable "flap" of two negatively charged amino acids (Glubeta397 and Aspbeta398) whose side chains are pinned back to the coiled coil with a calcium atom bridge until GHRPam occupies the beta-chain pocket. Additionally, in the absence of the peptide ligand GPRPam, GHRPam binds to the gamma-chain pocket, a new calcium-binding site being formed concomitantly.

PubMed: 10074346
DOI: 10.1021/bi982626w

実験手法

X-RAY DIFFRACTION (2.5 Å)