1DEQ

THE CRYSTAL STRUCTURE OF MODIFIED BOVINE FIBRINOGEN (AT ~4 ANGSTROM RESOLUTION)

Summary for 1DEQ

• Entry DOI: 10.2210/pdb1deq/pdb
• Related: 1FZA
• Descriptor: FIBRINOGEN (ALPHA CHAIN), FIBRINOGEN (BETA CHAIN), FIBRINOGEN (GAMMA CHAIN), ... (4 entities in total)
• Functional Keywords: coiled-coil, blood clotting
• Biological source: Bos taurus (cattle); More
• Cellular location: Secreted: P02672 P02676 P12799
• Total number of polymer chains: 14
• Total formula weight: 560537.53

Authors

Brown, J.H.,Volkmann, N.,Jun, G.,Henschen-Edman, A.H.,Cohen, C. (deposition date: 1999-11-15, release date: 2000-02-02, Last modification date: 2023-08-09)

Primary citation

Brown, J.H.,Volkmann, N.,Jun, G.,Henschen-Edman, A.H.,Cohen, C.
The crystal structure of modified bovine fibrinogen.
Proc.Natl.Acad.Sci.USA, 97:85-90, 2000

PubMed Abstract: Here we report the crystal structure at approximately 4-A resolution of a selectively proteolyzed bovine fibrinogen. This key component in hemostasis is an elongated 340-kDa glycoprotein in the plasma that upon activation by thrombin self-assembles to form the fibrin clot. The crystals are unusual because they are made up of end-to-end bonded molecules that form flexible filaments. We have visualized the entire coiled-coil region of the molecule, which has a planar sigmoidal shape. The primary polymerization receptor pockets at the ends of the molecule face the same way throughout the end-to-end bonded filaments, and based on this conformation, we have developed an improved model of the two-stranded protofibril that is the basic building block in fibrin. Near the middle of the coiled-coil region, the plasmin-sensitive segment is a hinge about which the molecule adopts different conformations. This segment also includes the boundary between the three- and four-stranded portions of the coiled coil, indicating the location on the backbone that anchors the extended flexible Aalpha arm. We suggest that a flexible branch point in the molecule may help accommodate variability in the structure of the fibrin clot.

PubMed: 10618375
DOI: 10.1073/pnas.97.1.85

Experimental method

X-RAY DIFFRACTION (3.5 Å)