Leech antihemostatic proteins share the T-knot scaffold, a disulfide-reinforced structural motif.
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.
Ascenzi
P
P
Department of Biology, Third University of Rome, Italy.
Bolognesi
M
M
Catalucci
D
D
Pascarella
S
S
Ruoppolo
M
M
Rizzi
M
M
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
D000925:Anticoagulants; D006629:Hirudins; D014361:Trypsin Inhibitors; D004815:Epidermal Growth Factor