期刊
BIOCHEMISTRY
卷 41, 期 40, 页码 12124-12132出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi0261894
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资金
- NHLBI NIH HHS [HL 31048] Funding Source: Medline
We report two crystal structures, each at a resolution of 2.8 Angstrom, of recombinant human fibrinogen fragment D (rtD) in the absence and presence of peptide ligands. The bound ligands, Gly-Pro-Arg-Pro-amide and Gly-His-Arg-Pro-amide, mimic the interactions of the thrombin exposed polymerization sites, A and B, respectively. This report is the first to describe the structure of fragment D in the presence of both peptide ligands. The structures reveal that recombinant fibrinogen is nearly identical to the plasma protein but with minor changes, like the addition of a proximal fucose to the carbohydrate linked to residue betaGln364, and slightly different relative positions of the beta- and gamma-modules. Of major interest in our structures is that a previously identified calcium site in plasma fibrinogen is absent when Gly-His-Arg-Pro-amide is bound. The peptide-dependent loss of this calcium site may have significant biological implications that are further discussed. These structures provide a foundation for the detailed structural analysis of variant recombinant fibrinogens that were used to identify critical functional residues within fragment D.
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