CRYSTAL-STRUCTURES OF FRAGMENT-D FROM HUMAN FIBRINOGEN AND ITS CROSS-LINKED COUNTERPART FROM FIBRIN

Citation
G. Spraggon et al., CRYSTAL-STRUCTURES OF FRAGMENT-D FROM HUMAN FIBRINOGEN AND ITS CROSS-LINKED COUNTERPART FROM FIBRIN, Nature, 389(6650), 1997, pp. 455-462
Citations number
50
Categorie Soggetti
Multidisciplinary Sciences
Journal title
NatureACNP
ISSN journal
00280836
Volume
389
Issue
6650
Year of publication
1997
Pages
455 - 462
Database
ISI
SICI code
0028-0836(1997)389:6650<455:COFFHF>2.0.ZU;2-D
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 cove fragment ( fragment D) from human fibrinogen has now been determined to 2.9 Angst rom resolution. The 86K three-chained structure consists of a coiled-c oil region and two homologous globular entities oriented at approximat ely 130 degrees to each other, Additionally, the covalently bound dime r of fragment D, known as 'doubte-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 sol ved by molecular replacement with the model of fragment D.