1lt9: Difference between revisions
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|PDB= 1lt9 |SIZE=350|CAPTION= <scene name='initialview01'>1lt9</scene>, resolution 2.80Å | |PDB= 1lt9 |SIZE=350|CAPTION= <scene name='initialview01'>1lt9</scene>, resolution 2.80Å | ||
|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=[[1fza|1FZA]], [[1fzb|1FZB]], [[1fzc|1FZC]], [[1fze|1FZE]], [[1fzf|1FZF]], [[1fzg|1FZG]], [[1ltj|1LTJ]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lt9 OCA], [http://www.ebi.ac.uk/pdbsum/1lt9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lt9 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
We report two crystal structures, each at a resolution of 2.8 A, of recombinant human fibrinogen fragment D (rfD) in the absence and presence of peptide ligands. The bound ligands, Gly-Pro-Arg-Pro-amide and Gly-His-Arg-Pro-amide, mimic the interactions of the thrombin exposed polymerization sites, "A" and "B", respectively. This report is the first to describe the structure of fragment D in the presence of both peptide ligands. The structures reveal that recombinant fibrinogen is nearly identical to the plasma protein but with minor changes, like the addition of a proximal fucose to the carbohydrate linked to residue betaGln364, and slightly different relative positions of the beta- and gamma-modules. Of major interest in our structures is that a previously identified calcium site in plasma fibrinogen is absent when Gly-His-Arg-Pro-amide is bound. The peptide-dependent loss of this calcium site may have significant biological implications that are further discussed. These structures provide a foundation for the detailed structural analysis of variant recombinant fibrinogens that were used to identify critical functional residues within fragment D. | We report two crystal structures, each at a resolution of 2.8 A, of recombinant human fibrinogen fragment D (rfD) in the absence and presence of peptide ligands. The bound ligands, Gly-Pro-Arg-Pro-amide and Gly-His-Arg-Pro-amide, mimic the interactions of the thrombin exposed polymerization sites, "A" and "B", respectively. This report is the first to describe the structure of fragment D in the presence of both peptide ligands. The structures reveal that recombinant fibrinogen is nearly identical to the plasma protein but with minor changes, like the addition of a proximal fucose to the carbohydrate linked to residue betaGln364, and slightly different relative positions of the beta- and gamma-modules. Of major interest in our structures is that a previously identified calcium site in plasma fibrinogen is absent when Gly-His-Arg-Pro-amide is bound. The peptide-dependent loss of this calcium site may have significant biological implications that are further discussed. These structures provide a foundation for the detailed structural analysis of variant recombinant fibrinogens that were used to identify critical functional residues within fragment D. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Kostelansky, M S.]] | [[Category: Kostelansky, M S.]] | ||
[[Category: Lord, S T.]] | [[Category: Lord, S T.]] | ||
[[Category: blood coagulation]] | [[Category: blood coagulation]] | ||
[[Category: fibrinogen]] | [[Category: fibrinogen]] | ||
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[[Category: recombinant fibrinogen fragment d]] | [[Category: recombinant fibrinogen fragment d]] | ||
''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 22:07:06 2008'' | ||
