1DUG

STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER PROTEIN DRIVEN CRYSTALLIZATION

Summary for 1DUG

• Entry DOI: 10.2210/pdb1dug/pdb
• Descriptor: chimera of GLUTATHIONE S-TRANSFERASE-synthetic LINKEr-C-TERMINAL FIBRINOGEN GAMMA CHAIN, GLUTATHIONE (3 entities in total)
• Functional Keywords: gamma chain integrin fragment, carrier protein driven crystallization, transferase, blood clotting
• Biological source: Schistosoma japonicum; More
• Cellular location: Secreted : P02679
• Total number of polymer chains: 2
• Total formula weight: 54881.36

Authors

Ware, S.,Donahue, J.P.,Hawiger, J.,Anderson, W.F. (deposition date: 2000-01-17, release date: 2000-02-02, Last modification date: 2024-02-07)

Primary citation

Ware, S.,Donahue, J.P.,Hawiger, J.,Anderson, W.F.
Structure of the fibrinogen gamma-chain integrin binding and factor XIIIa cross-linking sites obtained through carrier protein driven crystallization.
Protein Sci., 8:2663-2671, 1999

PubMed 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.

PubMed: 10631982

Experimental method

X-RAY DIFFRACTION (1.8 Å)