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Thromb Haemost 1999; 82(02): 271-276
DOI: 10.1055/s-0037-1615842
Research Article
Schattauer GmbH

Crystal Structures of Fragments D and Double-D from Fibrinogen and Fibrin

Russell F. Doolittle
1   Center for Molecular Genetics, University of California, San Diego, Novaritis Institute of Functional Genomics, San Diego, CA, USA, and Department of Biochemistry, University of Vermont School of Medicine, Burlington, VT, USA
,
Glen Spraggon
1   Center for Molecular Genetics, University of California, San Diego, Novaritis Institute of Functional Genomics, San Diego, CA, USA, and Department of Biochemistry, University of Vermont School of Medicine, Burlington, VT, USA
,
Stephen J. Everse
1   Center for Molecular Genetics, University of California, San Diego, Novaritis Institute of Functional Genomics, San Diego, CA, USA, and Department of Biochemistry, University of Vermont School of Medicine, Burlington, VT, USA
› Author Affiliations
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Publication History

Publication Date:
09 December 2017 (online)

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Introduction

After a long period of anticipation,1 the last two years have witnessed the first high-resolution x-ray structures of fragments from fibrinogen and fibrin.2-7 The results confirmed many aspects of fibrinogen structure and function that had previously been inferred from electron microscopy and biochemistry and revealed some unexpected features. Several matters have remained stubbornly unsettled, however, and much more work remains to be done. Here, we review several of the most significant findings that have accompanied the new x-ray structures and discuss some of the problems of the fibrinogen-fibrin conversion that remain unresolved.

* Abbreviations: GPR—Gly-Pro-Arg-derivatives; GPRPam—Gly-Pro-Arg-Pro-amide; GHRPam—Gly-His-Arg-Pro-amide

 

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