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• W1858651199 abstract "Research Article16 December 1996free access Crystal structure of a coagulogen, the clotting protein from horseshoe crab: a structural homologue of nerve growth factor. A. Bergner A. Bergner Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany. Search for more papers by this author V. Oganessyan V. Oganessyan Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany. Search for more papers by this author T. Muta T. Muta Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany. Search for more papers by this author S. Iwanaga S. Iwanaga Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany. Search for more papers by this author D. Typke D. Typke Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany. Search for more papers by this author R. Huber R. Huber Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany. Search for more papers by this author W. Bode W. Bode Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany. Search for more papers by this author A. Bergner A. Bergner Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany. Search for more papers by this author V. Oganessyan V. Oganessyan Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany. Search for more papers by this author T. Muta T. Muta Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany. Search for more papers by this author S. Iwanaga S. Iwanaga Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany. Search for more papers by this author D. Typke D. Typke Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany. Search for more papers by this author R. Huber R. Huber Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany. Search for more papers by this author W. Bode W. Bode Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany. Search for more papers by this author Author Information A. Bergner1, V. Oganessyan1, T. Muta1, S. Iwanaga1, D. Typke1, R. Huber1 and W. Bode1 1Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany. The EMBO Journal (1996)15:6789-6797https://doi.org/10.1002/j.1460-2075.1996.tb01070.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The clotting cascade system of the horseshoe crab (Limulus) is involved in both haemostasis and host defence. The cascade results in the conversion of coagulogen, a soluble protein, into an insoluble coagulin gel. The clotting enzyme excises the fragment peptide C from coagulogen, giving rise to aggregation of the monomers. The crystal structure of coagulogen reveals an elongated molecule that embraces the helical peptide C fragment. Cleavage and removal of the peptide C would expose an extended hydrophobic cove, which could interact with the hydrophobic edge of a second molecule, leading to a polymeric fibre. The C-terminal half of the coagulogen molecule exhibits a striking topological similarity to the neurotrophin nerve growth factor (NGF), providing the first evidence for a neurotrophin fold in invertebrates. Similarities between coagulogen and Spatzle, the Drosophila ligand of the receptor Toll, suggest that the neurotrophin fold might be considered more ancient and widespread than previously realized. Previous ArticleNext Article Volume 15Issue 241 December 1996In this issue RelatedDetailsLoading ..." @default.
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• W1858651199 title "Crystal structure of a coagulogen, the clotting protein from horseshoe crab: a structural homologue of nerve growth factor." @default.
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