Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.8
Classification:transferase, blood clotting
Release Date:2000-02-02
Deposition Date:2000-01-17
Revision Date:2008-04-27#2011-07-13#2017-08-09#2018-01-31
Molecular Weight:54881.36
Macromolecule Type:Protein
Residue Count:468
Atom Site Count:3858
DOI:10.2210/pdb1dug/pdb
Abstract:
The human fibrinogen gamma-chain C-terminal segment functions as the platelet integrin binding site as well as the Factor XIIIa cross-linking substrate and thus plays an important role in blood clot formation and stabilization. The three-dimensional structure of this segment has been determined using carrier protein driven crystallization. The C-terminal segment, gamma-(398-411), was attached to a linker sequence at the C-terminus of glutathione S-transferase and the structure of this fusion protein determined at 1.8 A resolution. Functional studies of the chimeric protein demonstrate that the fibrinogen sequence in the presence of the carrier protein retains its specific functions as ligand for platelet integrin alpha(IIb)beta3 (gpIIb/IIIa) and as a cross-linking substrate for Factor XIIIa. The structure obtained for the fibrinogen gamma-chain segment is not affected by crystal packing and can provide the missing links to the recently reported model of cross-linked fibrin.
Resolution:1.8
Classification:transferase, blood clotting
Release Date:2000-02-02
Deposition Date:2000-01-17
Revision Date:2008-04-27#2011-07-13#2017-08-09#2018-01-31
Molecular Weight:54881.36
Macromolecule Type:Protein
Residue Count:468
Atom Site Count:3858
DOI:10.2210/pdb1dug/pdb
Abstract:
The human fibrinogen gamma-chain C-terminal segment functions as the platelet integrin binding site as well as the Factor XIIIa cross-linking substrate and thus plays an important role in blood clot formation and stabilization. The three-dimensional structure of this segment has been determined using carrier protein driven crystallization. The C-terminal segment, gamma-(398-411), was attached to a linker sequence at the C-terminus of glutathione S-transferase and the structure of this fusion protein determined at 1.8 A resolution. Functional studies of the chimeric protein demonstrate that the fibrinogen sequence in the presence of the carrier protein retains its specific functions as ligand for platelet integrin alpha(IIb)beta3 (gpIIb/IIIa) and as a cross-linking substrate for Factor XIIIa. The structure obtained for the fibrinogen gamma-chain segment is not affected by crystal packing and can provide the missing links to the recently reported model of cross-linked fibrin.
| Date made available | 2000 |
|---|---|
| Publisher | RCSB-PDB |