The occcurence 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.

Leech antihemostatic proteins share the T-knot scaffold, a disulfide-reinforced structural motif / P., Ascenzi; M., Bolognesi; D., Catalucci; Pascarella, Stefano; M., Ruoppolo; M., Rizzi. - In: BIOLOGICAL CHEMISTRY. - ISSN 1431-6730. - STAMPA. - 379:11(1998), pp. 1387-1389. [10.1515/bchm.1998.379.11.1355, //1998]

Leech antihemostatic proteins share the T-knot scaffold, a disulfide-reinforced structural motif

PASCARELLA, Stefano;
1998

Abstract

The occcurence 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.
1998
antistasin; decorsin; egf-like proteins; hirudin; knottins; t-knot scaffold
01 Pubblicazione su rivista::01a Articolo in rivista
Leech antihemostatic proteins share the T-knot scaffold, a disulfide-reinforced structural motif / P., Ascenzi; M., Bolognesi; D., Catalucci; Pascarella, Stefano; M., Ruoppolo; M., Rizzi. - In: BIOLOGICAL CHEMISTRY. - ISSN 1431-6730. - STAMPA. - 379:11(1998), pp. 1387-1389. [10.1515/bchm.1998.379.11.1355, //1998]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/68549
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