1M1J

Crystal structure of native chicken fibrinogen with two different bound ligands

「1JFE」から置き換えられました

1M1J の概要

• エントリーDOI: 10.2210/pdb1m1j/pdb
• 関連するPDBエントリー: 1EI3 1FZC
• 分子名称: Fibrinogen alpha subunit, Fibrinogen beta chain, Fibrinogen gamma chain, ... (8 entities in total)
• 機能のキーワード: coiled coils, disulfide rings, fibrinogen, blood clotting
• 由来する生物種: Gallus gallus (chicken); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 311778.33

構造登録者

Yang, Z.,Kollman, J.M.,Pandi, L.,Doolittle, R.F. (登録日: 2002-06-19, 公開日: 2002-06-26, 最終更新日: 2024-10-30)

主引用文献

Yang, Z.,Kollman, J.M.,Pandi, L.,Doolittle, R.F.
Crystal Structure of Native Chicken Fibrinogen at 2.7 A Resolution
Biochemistry, 40:12515-12523, 2001

PubMed Abstract: The crystal structure of native chicken fibrinogen (320 kDa) complexed with two synthetic peptides has been determined at a resolution of 2.7 A. The structure provides the first atomic-resolution view of the polypeptide chain arrangement in the central domain where the two halves of the molecule are joined, as well as of a putative thrombin-binding site. The amino-terminal segments of the alpha and beta chains, including fibrinopeptides A and B, are not visible in electron density maps, however, and must be highly disordered. The alphaC domain is also very disordered. A residue by residue analysis of the coiled coils with regard to temperature factor shows a strong correlation between mobility and plasmin attack sites. It is concluded that structural flexibility is an inherent feature of fibrinogen that plays a key role in both its conversion to fibrin and its subsequent destruction by plasmin.

PubMed: 11601975
DOI: 10.1021/bi011394p

実験手法

X-RAY DIFFRACTION (2.7 Å)