Structural Alterations in Hereditary Dysfibrinogens

Author(s): Teruko Sugo, Yoichi Sakata, Michio Matsuda

Journal Name: Current Protein & Peptide Science

Volume 3 , Issue 3 , 2002

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Dysfibrinogens can be grossly divided in two groups: (1) defective thrombin-catalyzed conversion of fibrinogen molecules to fibrin monomers, and (2) defective fibrin polymerization due to structural alterations in polymerization sites, that include “A” and “a” sites, end-to-end D:D abutment surfaces, and lateral association sites involving the carboxyl terminal region of the fibrin α-chain. Recently, a number of mutations in the fibrinogen genes have been identified, and many of these encode changes that occur in regions of fibrinogen that have been elucidated by high-resolution structural studies. Here we focus on the structure-function relationships of fibrinogen that can be inferred from studies involving these abnormal molecules.

Keywords: dysfibrinogens, gamma275, alpha-16, dysfibrogenernias, d:d interface

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Article Details

Year: 2002
Page: [239 - 247]
Pages: 9
DOI: 10.2174/1389203023380648
Price: $65

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