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A Model of Fibrin Formation Based on Crystal Structures of Fibrinogen and Fibrin Fragments Complexed with Synthetic Peptides

Zhe Yang, Igor Mochalkin and Russell F. Doolittle
Proceedings of the National Academy of Sciences of the United States of America
Vol. 97, No. 26 (Dec. 19, 2000), pp. 14156-14161
Stable URL: http://www.jstor.org/stable/2666264
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
A Model of Fibrin Formation Based on Crystal Structures of Fibrinogen and Fibrin Fragments Complexed with Synthetic Peptides
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Abstract

A blood clot is a meshwork of fibrin fibers built up by the systematic assembly of fibrinogen molecules proteolyzed by thrombin. Here, we describe a model of how the assembly process occurs. Five kinds of interaction are explicitly defined, including two different knob-hole interactions, an end-to-end association between γ-chains, a lateral association between γ-chains, and a hypothetical lateral interaction between β-chains. The last two of these interactions are responsible for protofibril association and are predicated on intermolecular packing arrangements observed in crystal structures of fibrin double-D fragments cocrystallized with synthetic peptides corresponding to the knobs exposed by the release of the fibrinopeptides A and B.

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