Structural basis of the fibrinogen-fibrin transformation: contributions from X-ray crystallography.
During the past several years, a number of crystal structures have been determined of fragments from fibrinogen and fibrin and, most recently, a structure of a native fibrinogen. One feature of the fibrinogen molecule that has emerged from these studies has to do with its "loose ends," segments of the molecule that are extremely mobile and not discernable by X-ray crystallography. Some, if not all, of this flexibility is functionally important. Small synthetic peptides based on mobile parts of fibrinogen exposed by the action of thrombin have contributed significantly to these studies and may yet prove useful therapeutically. In the end, although crystal structures have added greatly to our understanding of fibrin formation, much still needs to be unraveled about how clots form.
Doolittle
Russell F
RF
Center for Molecular Genetics, University of California, San Diego, La Jolla 92093, USA. rdoolittle@ucsd.edu
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D005337:Fibrin / Q000737:chemistry*; D005338:Fibrin Fibrinogen Degradation Products / Q000737:chemistry; D005340:Fibrinogen / Q000737:chemistry*; D006801:Humans; D011487:Protein Conformation
D005338:Fibrin Fibrinogen Degradation Products; D005337:Fibrin; D005340:Fibrinogen