PDBsum entry 1ltj

Blood clotting

PDB id: 1ltj

Contents

Protein chains

65 a.a. *

298 a.a. *

299 a.a. *

58 a.a. *

Ligands

GLY-PRO-ARG-PRO ×2

GLY-HIS-ARG-PRO ×2

NAG-NAG-FUC ×2

Metals

_CA ×4

Waters ×250

* Residue conservation analysis

References listed in PDB file

Key reference

• Title: 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.
• Authors: M.S.Kostelansky, L.Betts, O.V.Gorkun, S.T.Lord.
• Ref.: Biochemistry, 2002, 41, 12124-12132. [DOI no: 10.1021/bi0261894]
• PubMed id: 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.