The Primary Fibrin Polymerization Pocket: Three-Dimensional Structure of a 30-kDa C-Terminal γ Chain Fragment Complexed with the Peptide Gly-Pro-Arg-Pro
After vascular injury, a cascade of serine protease activations leads to the conversion of the soluble fibrinogen molecule into fibrin. The fibrin monomers then polymerize spontaneously and noncovalently to form a fibrin gel. The primary interaction of this polymerization reaction is between the new...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1997-07, Vol.94 (14), p.7176-7181 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Pratt, K. P. Cote, H. C. F. Chung, D. W. Stenkamp, R. E. Davie, E. W. |
| description | After vascular injury, a cascade of serine protease activations leads to the conversion of the soluble fibrinogen molecule into fibrin. The fibrin monomers then polymerize spontaneously and noncovalently to form a fibrin gel. The primary interaction of this polymerization reaction is between the newly exposed N-terminal Gly-Pro-Arg sequence of the α chain of one fibrin molecule and the C-terminal region of a γ chain of an adjacent fibrin(ogen) molecule. In this report, the polymerization pocket has been identified by determining the crystal structure of a 30-kDa C-terminal fragment of the fibrin(ogen) γ chain complexed with the peptide Gly-Pro-Arg-Pro. This peptide mimics the N terminus of the α chain of fibrin. The conformational change in the protein upon binding the peptide is subtle, with electrostatic interactions primarily mediating the association. This is consistent with biophysical experiments carried out over the last 50 years on this fundamental polymerization reaction. |
| doi_str_mv | 10.1073/pnas.94.14.7176 |
| format | Article |
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P. ; Cote, H. C. F. ; Chung, D. W. ; Stenkamp, R. E. ; Davie, E. W.</creator><creatorcontrib>Pratt, K. P. ; Cote, H. C. F. ; Chung, D. W. ; Stenkamp, R. E. ; Davie, E. W.</creatorcontrib><description>After vascular injury, a cascade of serine protease activations leads to the conversion of the soluble fibrinogen molecule into fibrin. The fibrin monomers then polymerize spontaneously and noncovalently to form a fibrin gel. The primary interaction of this polymerization reaction is between the newly exposed N-terminal Gly-Pro-Arg sequence of the α chain of one fibrin molecule and the C-terminal region of a γ chain of an adjacent fibrin(ogen) molecule. In this report, the polymerization pocket has been identified by determining the crystal structure of a 30-kDa C-terminal fragment of the fibrin(ogen) γ chain complexed with the peptide Gly-Pro-Arg-Pro. This peptide mimics the N terminus of the α chain of fibrin. The conformational change in the protein upon binding the peptide is subtle, with electrostatic interactions primarily mediating the association. 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P.</creatorcontrib><creatorcontrib>Cote, H. C. F.</creatorcontrib><creatorcontrib>Chung, D. W.</creatorcontrib><creatorcontrib>Stenkamp, R. E.</creatorcontrib><creatorcontrib>Davie, E. W.</creatorcontrib><title>The Primary Fibrin Polymerization Pocket: Three-Dimensional Structure of a 30-kDa C-Terminal γ Chain Fragment Complexed with the Peptide Gly-Pro-Arg-Pro</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>After vascular injury, a cascade of serine protease activations leads to the conversion of the soluble fibrinogen molecule into fibrin. The fibrin monomers then polymerize spontaneously and noncovalently to form a fibrin gel. The primary interaction of this polymerization reaction is between the newly exposed N-terminal Gly-Pro-Arg sequence of the α chain of one fibrin molecule and the C-terminal region of a γ chain of an adjacent fibrin(ogen) molecule. 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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1997-07, Vol.94 (14), p.7176-7181 |
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| source | MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry; JSTOR |
| subjects | Atoms Biochemistry Biological Sciences Crystal structure Crystallography Dimerization Fibrin - chemistry Fibrin - metabolism Hydrogen bonds Models, Molecular Molecular chains Molecular Sequence Data Molecular structure Molecules Nodules Oligopeptides - chemistry Oligopeptides - metabolism Peptides Polymerization Protein Conformation Proteins |
| title | The Primary Fibrin Polymerization Pocket: Three-Dimensional Structure of a 30-kDa C-Terminal γ Chain Fragment Complexed with the Peptide Gly-Pro-Arg-Pro |
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