title: Leech antihemostatic proteins share the T-knot scaffold, a disulfide-reinforced structural motif.
abstract: The occurrence of similar topologies among unrelated proteins is an emerging theme in structural biology. Here we report that the T-knot scaffold, a disulfide-reinforced structural motif shared by knottins and EGF-like proteins, is also present in leech antihemostatic proteins. Our finding emphasizes the versatile nature of this small structural motif, representing a compact structural unit suitable for the diverse biological functions performed by knottins, EGF-like proteins and leech antihemostatic proteins.
authors.affiliation: Department of Biology, Third University of Rome, Italy.
authors.forename: P
authors.initials: P
authors.lastname: Ascenzi
authors.forename: M
authors.initials: M
authors.lastname: Bolognesi
authors.forename: D
authors.initials: D
authors.lastname: Catalucci
authors.forename: S
authors.initials: S
authors.lastname: Pascarella
authors.forename: M
authors.initials: M
authors.lastname: Ruoppolo
authors.forename: M
authors.initials: M
authors.lastname: Rizzi
mesh_terms: D000818:Animals; D000925:Anticoagulants / Q000737:chemistry*; D004815:Epidermal Growth Factor / Q000737:chemistry; D006629:Hirudins / Q000737:chemistry; D006801:Humans; D007865:Leeches / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D014361:Trypsin Inhibitors / Q000737:chemistry
chemical_list: D000925:Anticoagulants; D006629:Hirudins; D014361:Trypsin Inhibitors; D004815:Epidermal Growth Factor