PDBsum entry: 1fza

Blood coagulation

PDB-id: 1fza

Asymmetric unit

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Description

Header details

Header records

References

PROCHECK

Protein chains

85 a.a. *

313 a.a. *

309 a.a. *

Ligands

NAG ×2

Metal ions

_CA ×2

* Residue conservation analysis

Tools

Clefts Calculation

Biological unit*, trimer
(*as deduced by PQS)

PDB id:

1fza

Name:

Blood coagulation

Title:

Crystal structure of fibrinogen fragment d

Structure:

Fibrinogen. Chain: a, d. Fragment: fragment d. Fibrinogen. Chain: b, e. Fragment: fragment d. Fibrinogen. Chain: c, f. Fragment: fragment d

Source:

Homo sapiens. Human. Organism_taxid: 9606. Organ: blood. Tissue: blood. Tissue: blood

Biological unit:

Trimer (from PQS)

UniProt:

Chains A, D: P02671 (FIBA_HUMAN)

Seq:
Struc:
	Seq:
	Struc:
Seq:
Struc:
	Seq:	866 a.a.
	Struc:	85 a.a.

Chains B, E: P02675 (FIBB_HUMAN)

Seq:
Struc:
	Seq:	491 a.a.
	Struc:	313 a.a.

Chains C, F: P02679 (FIBG_HUMAN)

Seq:

Struc:

Seq:

453 a.a.

Struc:

309 a.a.

Key:	PfamA domain	PfamB domain
Secondary structure	CATH domain

Resolution:

2.90Å

R-factor:

0.263

R-free:

0.363

Authors:

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

Key ref:

G.Spraggon et al. (1997). Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin.. Nature, 389, 455-462. [PubMed id: 9333233] [DOI: 10.1038/38947]

Date:

05-Aug-97

Release date:

03-Dec-97

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Key reference

DOI no: 10.1038/38947

Nature 389:455-462 (1997)

PubMed id: 9333233

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

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

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.

Selected figure(s)

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.

Figures were selected by an automated process.