3GHG

Crystal Structure of Human Fibrinogen

3GHG の概要

• エントリーDOI: 10.2210/pdb3ghg/pdb
• 関連するPDBエントリー: 1DEQ 1FZC 1M1J 2A45
• 分子名称: Fibrinogen alpha chain, Fibrinogen beta chain, Fibrinogen gamma chain, ... (9 entities in total)
• 機能のキーワード: triple-stranded coiled coil, beta sheets, alpha helices, amyloid, amyloidosis, blood coagulation, disease mutation, glycoprotein, phosphoprotein, secreted, pyrrolidone carboxylic acid, sulfation, blood clotting
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 651387.77

構造登録者

Doolittle, R.F.,Kollman, J.M.,Sawaya, M.R.,Pandi, L.,Riley, M. (登録日: 2009-03-03, 公開日: 2009-05-19, 最終更新日: 2024-11-06)

主引用文献

Kollman, J.M.,Pandi, L.,Sawaya, M.R.,Riley, M.,Doolittle, R.F.
Crystal structure of human fibrinogen.
Biochemistry, 48:3877-3886, 2009

PubMed Abstract: A crystal structure of human fibrinogen has been determined at approximately 3.3 A resolution. The protein was purified from human blood plasma, first by a cold ethanol precipitation procedure and then by stepwise chromatography on DEAE-cellulose. A product was obtained that was homogeneous on SDS-polyacrylamide gels. Nonetheless, when individual crystals used for X-ray diffraction were examined by SDS gel electrophoresis after data collection, two species of alpha chain were present, indicating that some proteolysis had occurred during the course of operations. Amino-terminal sequencing on post-X-ray crystals showed mostly intact native alpha- and gamma-chain sequences (the native beta chain is blocked). The overall structure differs from that of a native fibrinogen from chicken blood and those reported for a partially proteolyzed bovine fibrinogen in the nature of twist in the coiled-coil regions, likely due to weak forces imparted by unique crystal packing. As such, the structure adds to the inventory of possible conformations that may occur in solution. Other features include a novel interface with an antiparallel arrangement of beta chains and a unique tangential association of coiled coils from neighboring molecules. The carbohydrate groups attached to beta chains are unusually prominent, the full sweep of 11 sugar residues being positioned. As was the case for native chicken fibrinogen, no resolvable electron density could be associated with alphaC domains.

PubMed: 19296670
DOI: 10.1021/bi802205g

実験手法

X-RAY DIFFRACTION (2.9 Å)