1ltj

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(New page: 200px<br /> <applet load="1ltj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ltj, resolution 2.80&Aring;" /> '''Crystal Structure o...)
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<applet load="1ltj" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Crystal Structure of Recombinant Human Fibrinogen Fragment D with the Peptide Ligands Gly-Pro-Arg-Pro-Amide and Gly-His-Arg-Pro-Amide'''<br />
'''Crystal Structure of Recombinant Human Fibrinogen Fragment D with the Peptide Ligands Gly-Pro-Arg-Pro-Amide and Gly-His-Arg-Pro-Amide'''<br />
==Overview==
==Overview==
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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.
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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.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1LTJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LTJ OCA].
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1LTJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTJ OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Betts, L.]]
[[Category: Betts, L.]]
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[[Category: Gorkun, O.V.]]
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[[Category: Gorkun, O V.]]
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[[Category: Kostelansky, M.S.]]
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[[Category: Kostelansky, M S.]]
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[[Category: Lord, S.T.]]
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[[Category: Lord, S T.]]
[[Category: CA]]
[[Category: CA]]
[[Category: blood coagulation]]
[[Category: blood coagulation]]
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[[Category: recombinant fibrinogen fragment d with two peptide ligands]]
[[Category: recombinant fibrinogen fragment d with two peptide ligands]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:04:08 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:16 2008''

Revision as of 11:48, 21 February 2008


1ltj, resolution 2.80Å

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Crystal Structure of Recombinant Human Fibrinogen Fragment D with the Peptide Ligands Gly-Pro-Arg-Pro-Amide and Gly-His-Arg-Pro-Amide

Contents

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.

Disease

Known diseases associated with this structure: Afibrinogenemia, congenital OMIM:[134820], Afibrinogenemia, congenital OMIM:[134830], Amyloidosis, hereditary renal OMIM:[134820], Dysfibrinogenemia, alpha type, causing bleeding diathesis OMIM:[134820], Dysfibrinogenemia, alpha type, causing recurrent thrombosis OMIM:[134820], Dysfibrinogenemia, beta type OMIM:[134830], Dysfibrinogenemia, gamma type OMIM:[134850], Hypofibrinogenemia, gamma type OMIM:[134850], Thrombophilia, dysfibrinogenemic OMIM:[134830], Thrombophilia, dysfibrinogenemic OMIM:[134850]

About this Structure

1LTJ is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

2.8 A crystal structures of recombinant fibrinogen fragment D with and without two peptide ligands: GHRP binding to the "b" site disrupts its nearby calcium-binding site., Kostelansky MS, Betts L, Gorkun OV, Lord ST, Biochemistry. 2002 Oct 8;41(40):12124-32. PMID:12356313

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