1LT9

Crystal Structure of Recombinant Human Fibrinogen Fragment D

1LT9 の概要

• エントリーDOI: 10.2210/pdb1lt9/pdb
• 関連するPDBエントリー: 1FZA 1FZB 1FZC 1FZE 1FZF 1FZG 1LTJ
• 分子名称: Fibrinogen alpha/alpha-E chain, Fibrinogen beta chain, Fibrinogen gamma chain, ... (6 entities in total)
• 機能のキーワード: blood coagulation, fibrinogen, fibrinogen fragment d, recombinant fibrinogen fragment d, recombinant fibrinogen, blood clotting
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 158493.36

構造登録者

Kostelansky, M.S.,Betts, L.,Gorkun, O.V.,Lord, S.T. (登録日: 2002-05-20, 公開日: 2002-11-06, 最終更新日: 2024-11-13)

主引用文献

Kostelansky, M.S.,Betts, L.,Gorkun, O.V.,Lord, S.T.
2.8 A Crystal Structures of Recombinant Fibrinogen Fragment D with and without Two Peptide Ligands: GHRP Binding to the "b" Site Disrupts Its Nearby Calcium-binding Site.
Biochemistry, 41:12124-12132, 2002

PubMed Abstract: We report two crystal structures, each at a resolution of 2.8 A, of recombinant human fibrinogen fragment D (rfD) in the absence and presence of peptide ligands. The bound ligands, Gly-Pro-Arg-Pro-amide and Gly-His-Arg-Pro-amide, mimic the interactions of the thrombin exposed polymerization sites, "A" and "B", respectively. This report is the first to describe the structure of fragment D in the presence of both peptide ligands. The structures reveal that recombinant fibrinogen is nearly identical to the plasma protein but with minor changes, like the addition of a proximal fucose to the carbohydrate linked to residue betaGln364, and slightly different relative positions of the beta- and gamma-modules. Of major interest in our structures is that a previously identified calcium site in plasma fibrinogen is absent when Gly-His-Arg-Pro-amide is bound. The peptide-dependent loss of this calcium site may have significant biological implications that are further discussed. These structures provide a foundation for the detailed structural analysis of variant recombinant fibrinogens that were used to identify critical functional residues within fragment D.

PubMed: 12356313
DOI: 10.1021/bi0261894

実験手法

X-RAY DIFFRACTION (2.8 Å)