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2.8 A Crystal Structures of Recombinant Fibrinogen Fragment D With and Without Two Peptide Ligands: GHRP Binding to the "B" Site Disrupts Its Nearby Calcium-Binding Site

2.8 A Crystal Structures of Recombinant Fibrinogen Fragment D With and Without Two Peptide Ligands: GHRP Binding to the "B" Site Disrupts Its Nearby Calcium-Binding Site

Michael S Kostelansky, Laurie Betts, Oleg V Gorkun, Susan T Lord

Biochemistry. 2002 Oct 8;41(40):12124-32.

PMID: 12356313

Abstract:

We report two crystal structures, each at a resolution of 2.8 A, of recombinant human fibrinogen fragment D (rfD) 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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP126047754	Gly-Pro-Arg-Pro amide		126047-75-4	Price

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