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Thromb Haemost 1998; 80(01): 1-9
DOI: 10.1055/s-0037-1615130
Review Articles
Schattauer GmbH

A Three-Dimensional Consideration of Variant Human Fibrinogens

Stephen J. Everse
1   From the Center for Molecular Genetics, Univ. California, San Diego, La Jolla, CA, USA
,
Glen Spraggon
1   From the Center for Molecular Genetics, Univ. California, San Diego, La Jolla, CA, USA
,
Russell F. Doolittle
1   From the Center for Molecular Genetics, Univ. California, San Diego, La Jolla, CA, USA
› Author Affiliations
Further Information

Publication History

Received 23 December 1997

Accepted after resubmission 16 March 1998

Publication Date:
08 December 2017 (online)

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Summary

Recently reported X-ray structures for large core fragments derived from human fibrinogen and fibrin make it possible to correlate structural and functional anomalies of known genetic variants. Here we examine a variety of amino acid replacements previously reported for hereditary dysfibrinogenemias, most of which are associated with impaired fibrin polymerization. For many of these we have modeled in the mutant amino acid and considered the structural consequences. We have also examined the cases of a small deletion and a large insertion, as well as the impact of substitutions in the GPRPam ligand that was co-crystallized with fragment double-D.

 

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