PDBsum entry 1fzb

Blood coagulation

PDB id: 1fzb

Contents

Protein chains

81 a.a. *

312 a.a. *

309 a.a. *

Ligands

GLY-PRO-ARG-PRO ×2

NAG ×2

Metals

_CA ×2

* Residue conservation analysis

References listed in PDB file

Key reference

Title

Crystal structures of fragment d from human fibrinogen and its crosslinked counterpart from fibrin.

Authors

G.Spraggon, S.J.Everse, R.F.Doolittle.

Ref.

Nature, 1997, 389, 455-462. [DOI no: 10.1038/38947]

PubMed id

9333233

Abstract

In blood coagulation, units of the protein fibrinogen pack together to form a fibrin clot, but a crystal structure for fibrinogen is needed to understand how this is achieved. The structure of a core fragment (fragment D) from human fibrinogen has now been determined to 2.9 A resolution. The 86K three-chained structure consists of a coiled-coil region and two homologous globular entitles oriented at approximately 130 degrees to each other. Additionally, the covalently bound dimer of fragment D, known as 'double-D', was isolated from human fibrin, crystallized in the presence of a Gly-Pro-Arg-Pro-amide peptide ligand, which simulates the donor polymerization site, and its structure solved by molecular replacement with the model of fragment D.

Figure 4.
Figure 4 a, Topology of -chain (green) and -chain (red) C-terminal domains. The first residue in each segment of secondary structure is numbered. b, Stereo depiction of superposed C backbone structures from globular portions of -chains (green) and -chains (red); the numbers on the strands and letters on the helices correspond to the secondary structure designations in Fig. 4. c, GRASP representation of binding cavities of -chains (left) and -chains (right) showing charge distribution; red, negatively charged; blue, positively charged^47. Domains have been reorientated to show equivalent projections.

Figure 5.
Figure 5 a, Topology of -chain (green) and -chain (red) C-terminal domains. The first residue in each segment of secondary structure is numbered. b, Stereo depiction of superposed C backbone structures from globular portions of -chains (green) and -chains (red); the numbers on the strands and letters on the helices correspond to the secondary structure designations in Fig. 4. c, GRASP representation of binding cavities of -chains (left) and -chains (right) showing charge distribution; red, negatively charged; blue, positively charged^47. Domains have been reorientated to show equivalent projections.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nature (1997, 389, 455-462) copyright 1997.