1dug: Difference between revisions
New page: left|200px<br /> <applet load="1dug" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dug, resolution 1.80Å" /> '''STRUCTURE OF THE FI... |
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caption="1dug, resolution 1.80Å" /> | caption="1dug, resolution 1.80Å" /> | ||
'''STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER PROTEIN DRIVEN CRYSTALLIZATION'''<br /> | '''STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER PROTEIN DRIVEN CRYSTALLIZATION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1DUG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schistosoma_japonicum Schistosoma japonicum] with GSH as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | 1DUG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schistosoma_japonicum Schistosoma japonicum] with <scene name='pdbligand=GSH:'>GSH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUG OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: gamma chain integrin fragment]] | [[Category: gamma chain integrin fragment]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:40:47 2008'' |
Revision as of 16:40, 15 February 2008
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STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER PROTEIN DRIVEN CRYSTALLIZATION
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Dysfibrinogenemia, gamma type OMIM:[134850], Hypofibrinogenemia, gamma type OMIM:[134850], Thrombophilia, dysfibrinogenemic OMIM:[134850]
About this StructureAbout this Structure
1DUG is a Single protein structure of sequence from Schistosoma japonicum with as ligand. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.
ReferenceReference
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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