1fza: Difference between revisions
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[[Image:1fza.jpg|left|200px]] | [[Image:1fza.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF FIBRINOGEN FRAGMENT D''' | {{Structure | ||
|PDB= 1fza |SIZE=350|CAPTION= <scene name='initialview01'>1fza</scene>, resolution 2.9Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF FIBRINOGEN FRAGMENT D''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1FZA is a [ | 1FZA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FZA OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9333233 9333233] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: platelet]] | [[Category: platelet]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:15:57 2008'' |
Revision as of 12:15, 20 March 2008
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, resolution 2.9Å | |||||||
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Ligands: | and | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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
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