1dug: Difference between revisions

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[[Image:1dug.jpg|left|200px]]
{{Seed}}
[[Image:1dug.png|left|200px]]


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{{STRUCTURE_1dug|  PDB=1dug  |  SCENE=  }}  
{{STRUCTURE_1dug|  PDB=1dug  |  SCENE=  }}  


'''STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER PROTEIN DRIVEN CRYSTALLIZATION'''
===STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER PROTEIN DRIVEN CRYSTALLIZATION===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_10631982}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_10631982}}


==About this Structure==
==About this Structure==
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[[Category: Carrier protein driven crystallization]]
[[Category: Carrier protein driven crystallization]]
[[Category: Gamma chain integrin fragment]]
[[Category: Gamma chain integrin fragment]]
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