Gronwald, Wolfram and Bomke, Joerg and Maurer, Till and Domogalla, Barbara and Huber, Fritz and Schumann, Frank and Kremer, Werner and Fink, Florian and Rysiok, Thomas and Frech, Matthias and Kalbitzer, Hans Robert (2008) Structure of the leech protein saratin and characterization of its binding to collagen. JOURNAL OF MOLECULAR BIOLOGY, 381 (4). pp. 913-927. ISSN 0022-2836,
Full text not available from this repository. (Request a copy)Abstract
The leech protein Saratin from Hirudo medicinalis prevents thrombocyte aggregation by interfering with the first binding step of the thrombocytes to collagen by binding to collagen. We solved the three-dimensional structure of the leech protein Saratin in solution and identified its collagen binding site by NMR titration experiments. The NMR structure of Saratin consists of one alpha-helix and a five-stranded beta-sheet arranged in the topology The C-terminal region, of about 20 amino acids in length, adopts no regular structure. NMR titration experiments with collagen peptides show that the collagen interaction of Saratin takes place in a kind of notch that is formed by the end of the alpha-helix and the beta-sheet. NMR data-driven docking experiments to collagen model peptides were used to elucidate the Putative binding mode of Saratin and collagen. Mainly, parts of the first and the end of the fifth beta-strand, the loop connecting the alpha-helix and the third strand, and a short part of the loop connecting the fourth and fifth beta-strand participate in binding. (C) 2008 Elsevier Ltd. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | VON-WILLEBRAND-FACTOR; MAGNETIC-RESONANCE RELAXATION; DEPENDENT PLATELET-ADHESION; MODEL-FREE APPROACH; FACTOR A1 DOMAIN; CRYSTAL-STRUCTURE; CHEMICAL-SHIFT; SECONDARY STRUCTURE; GLYCOPROTEIN IB; NMR STRUCTURES; saratin structure; collagen interaction; leech protein; NMR; hemostasis |
| Subjects: | 500 Science > 570 Life sciences 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Institut für Funktionelle Genomik > Lehrstuhl für Funktionelle Genomik (Prof. Oefner) Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 26 Oct 2020 06:53 |
| Last Modified: | 26 Oct 2020 06:53 |
| URI: | https://pred.uni-regensburg.de/id/eprint/30288 |
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