1fzb: Difference between revisions
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|PDB= 1fzb |SIZE=350|CAPTION= <scene name='initialview01'>1fzb</scene>, resolution 2.9Å | |PDB= 1fzb |SIZE=350|CAPTION= <scene name='initialview01'>1fzb</scene>, resolution 2.9Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fzb OCA], [http://www.ebi.ac.uk/pdbsum/1fzb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fzb RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Everse, S J.]] | [[Category: Everse, S J.]] | ||
[[Category: Spraggon, G.]] | [[Category: Spraggon, G.]] | ||
[[Category: blood coagulation]] | [[Category: blood coagulation]] | ||
[[Category: fibrin]] | [[Category: fibrin]] | ||
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[[Category: platelet]] | [[Category: platelet]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:33:13 2008'' | ||
Revision as of 17:33, 30 March 2008
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| 1fzb, resolution 2.9Å | |||||||||||||
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| Ligands: | CA, NAG | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF CROSSLINKED FRAGMENT D
Overview
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.
About this Structure
1FZB is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
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:9333233
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