PDBsum entry 1dug

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Top Page protein ligands Protein-protein interface(s) links
Transferase, blood clotting PDB id
Protein chains
234 a.a. *
GSH ×2
Waters ×662
* Residue conservation analysis

References listed in PDB file
Key reference
Title Structure of the fibrinogen gamma-Chain integrin binding and factor xiiia cross-Linking sites obtained through carrier protein driven crystallization.
Authors S.Ware, J.P.Donahue, J.Hawiger, W.F.Anderson.
Ref. Protein Sci, 1999, 8, 2663-2671. [DOI no: 10.1110/ps.8.12.2663]
PubMed id 10631982
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.
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