 | FIBRINOGEN: XVIth INTERNATIONAL FIBRINOGEN WORKSHOP
Copyright © 2001 by the New York Academy of Sciences
description
Annals of the New York Academy of Sciences 936:31-43 (2001)
© 2001 New York Academy of Sciences
Crystal Structure Studies on Fibrinogen and Fibrin
RUSSELL F. DOOLITTLE,
ZHE YANG AND
IGOR MOCHALKIN
Center for Molecular Genetics, University California, San Diego, La Jolla, California 92093, USA
Address for correspondence: R.F. Doolittle, Ph.D., Center for Molecular Genetics, Rm. 206, University of California, San Diego, La Jolla, CA 92093-0634, USA. Voice: 858-534-4417; fax: 858-534-4985.
rdoolittle{at}ucsd.edu
X-ray crystallography studies on fragments D and double-D from human fibrinogen and fibrin have revealed the details of knob-hole interactions between fibrin units, as well as the nature of the association at their ends. More recently, a lower-resolution structure of native chicken fibrinogen has provided details about the structure of the central domain, and particularly the arrangement of disulfide bonds. Parts of the fibrinogen molecule are so flexible that they have not been visualized in electron density maps. The elusive regions include the  C domain, the amino-terminal segments of the and ß chains, and the carboxyl-terminal segments of the  chains. Nonetheless, when all the structural data are considered together, it is possible to construct a realistic model not only of a fibrinogen molecule but also of a fibrin protofibril.
Key Words: Fibrinogen • Fibrin • Crystal structure • Synthetic peptide knobs • Protofibril model
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