1dug: Difference between revisions
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[[Image:1dug.jpg|left|200px]] | [[Image:1dug.jpg|left|200px]] | ||
'''STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER PROTEIN DRIVEN CRYSTALLIZATION''' | {{Structure | ||
|PDB= 1dug |SIZE=350|CAPTION= <scene name='initialview01'>1dug</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER PROTEIN DRIVEN CRYSTALLIZATION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DUG is a [ | 1DUG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Schistosoma_japonicum Schistosoma japonicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUG OCA]. | ||
==Reference== | ==Reference== | ||
Structure of the fibrinogen gamma-chain integrin binding and factor XIIIa cross-linking sites obtained through carrier protein driven crystallization., Ware S, Donahue JP, Hawiger J, Anderson WF, Protein Sci. 1999 Dec;8(12):2663-71. PMID:[http:// | Structure of the fibrinogen gamma-chain integrin binding and factor XIIIa cross-linking sites obtained through carrier protein driven crystallization., Ware S, Donahue JP, Hawiger J, Anderson WF, Protein Sci. 1999 Dec;8(12):2663-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10631982 10631982] | ||
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Schistosoma japonicum]] | [[Category: Schistosoma japonicum]] | ||
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[[Category: gamma chain integrin fragment]] | [[Category: gamma chain integrin fragment]] | ||
''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 10:44:29 2008'' | ||
Revision as of 08:44, 20 March 2008
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| 1dug, resolution 1.80Å | |||||||||||||
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| Ligands: | GSH | ||||||||||||
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER PROTEIN DRIVEN CRYSTALLIZATION
Overview
The human fibrinogen gamma-chain C-terminal segment functions as the platelet integrin binding site as well as the Factor XIIIa cross-linking substrate and thus plays an important role in blood clot formation and stabilization. The three-dimensional structure of this segment has been determined using carrier protein driven crystallization. The C-terminal segment, gamma-(398-411), was attached to a linker sequence at the C-terminus of glutathione S-transferase and the structure of this fusion protein determined at 1.8 A resolution. Functional studies of the chimeric protein demonstrate that the fibrinogen sequence in the presence of the carrier protein retains its specific functions as ligand for platelet integrin alpha(IIb)beta3 (gpIIb/IIIa) and as a cross-linking substrate for Factor XIIIa. The structure obtained for the fibrinogen gamma-chain segment is not affected by crystal packing and can provide the missing links to the recently reported model of cross-linked fibrin.
Disease
Known diseases associated with this structure: Dysfibrinogenemia, gamma type OMIM:[134850], Hypofibrinogenemia, gamma type OMIM:[134850], Thrombophilia, dysfibrinogenemic OMIM:[134850]
About this Structure
1DUG is a Single protein structure of sequence from Schistosoma japonicum. Full crystallographic information is available from OCA.
Reference
Structure of the fibrinogen gamma-chain integrin binding and factor XIIIa cross-linking sites obtained through carrier protein driven crystallization., Ware S, Donahue JP, Hawiger J, Anderson WF, Protein Sci. 1999 Dec;8(12):2663-71. PMID:10631982
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