Structure of the leech protein saratin and characterization of its binding to collagen
Research article published in Journal of molecular biology (2008)
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 betabetaalphabetabetabeta. 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 beta-strand, and a short part of the loop connecting the fourth and fifth beta-strand participate in binding.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Resumen
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.
Por qué esto importa para la hirudoterapia
Este estudio resolvió la estructura tridimensional por RMN en disolución de la Saratina, una proteína derivada de la sanguijuela Hirudo medicinalis que previene la agregación trombocitaria mediante la unión a colágeno, y caracterizó su sitio de unión a colágeno. La estructura comprende una alfa-hélice y una lámina beta de cinco hebras, y mediante titulación por RMN y experimentos de docking se identificó una hendidura de unión formada por el extremo de la alfa-hélice y la lámina beta, con implicación de hebras y bucles específicos. Esto es directamente relevante para el ámbito de la ASH, ya que esclarece la base estructural del mecanismo antitrombótico de una proteína del secretoma de la sanguijuela a nivel molecular. Sin embargo, se trata de un estudio estructural/bioquímico que utiliza péptidos de colágeno modelo, sin datos in vivo ni clínicos, por lo que las implicaciones terapéuticas quedan sin comprobar.
Citación
Structure of the leech protein saratin and characterization of its binding to collagen
Gronwald W et al. · Journal of molecular biology, 2008
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Añadido a la biblioteca ASH: May 27, 2026 · Última actualización del sitio: 18 de junio de 2026