1fza
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CRYSTAL STRUCTURE OF FIBRINOGEN FRAGMENT D
OverviewOverview
In blood coagulation, units of the protein fibrinogen pack together to, form a fibrin clot, but a crystal structure for fibrinogen is needed to, understand how this is achieved. The structure of a core fragment, (fragment D) from human fibrinogen has now been determined to 2.9 A, resolution. The 86K three-chained structure consists of a coiled-coil, region and two homologous globular entitles oriented at approximately 130, degrees to each other. Additionally, the covalently bound dimer of, fragment D, known as 'double-D', was isolated from human fibrin, crystallized in the presence of a Gly-Pro-Arg-Pro-amide peptide ligand, which simulates the donor polymerization site, and its structure solved by, molecular replacement with the model of fragment D.
DiseaseDisease
Known diseases associated with this structure: Afibrinogenemia, congenital OMIM:[134820], Afibrinogenemia, congenital OMIM:[134830], Amyloidosis, hereditary renal OMIM:[134820], Dysfibrinogenemia, alpha type, causing bleeding diathesis OMIM:[134820], Dysfibrinogenemia, alpha type, causing recurrent thrombosis OMIM:[134820], Dysfibrinogenemia, beta type OMIM:[134830], Dysfibrinogenemia, gamma type OMIM:[134850], Hypofibrinogenemia, gamma type OMIM:[134850], Thrombophilia, dysfibrinogenemic OMIM:[134830], Thrombophilia, dysfibrinogenemic OMIM:[134850]
About this StructureAbout this Structure
1FZA is a Protein complex structure of sequences from Homo sapiens with NAG and CA as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin., Spraggon G, Everse SJ, Doolittle RF, Nature. 1997 Oct 2;389(6650):455-62. PMID:9333233
Page seeded by OCA on Mon Nov 12 16:58:38 2007