1dug: Difference between revisions

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==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.

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==

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[[Category: Schistosoma japonicum]]

[[Category: Single protein]]

[[Category: Anderson, W.F.]]

[[Category: Anderson, W F.]]

[[Category: Donahue, J.P.]]

[[Category: Donahue, J P.]]

[[Category: Hawiger, J.]]

[[Category: Ware, S.]]

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[[Category: gamma chain integrin fragment]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:35 2008''

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 17: / Line 17: @@
 [[Category: Schistosoma japonicum]]
 [[Category: Single protein]]
-[[Category: Anderson, W.F.]]
+[[Category: Anderson, W F.]]
-[[Category: Donahue, J.P.]]
+[[Category: Donahue, J P.]]
 [[Category: Hawiger, J.]]
 [[Category: Ware, S.]]
@@ Line 25: / Line 25: @@
 [[Category: gamma chain integrin fragment]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:40:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:35 2008''