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

Paolo Ascenzi, Martino Bolognesi, Daniele Catalucci, Stefano Pascarella, Margherita Ruoppolo, Menico Rizzi

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)1387-1389
Number of pages3
JournalBiological Chemistry
Volume379
Issue number11
Publication statusPublished - 1998

Keywords

  • Antistasin
  • Decorsin
  • EGF-like proteins
  • Hirudin
  • Knottins
  • T-knot scaffold

ASJC Scopus subject areas

  • Biochemistry

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  • Cite this

    Ascenzi, P., Bolognesi, M., Catalucci, D., Pascarella, S., Ruoppolo, M., & Rizzi, M. (1998). Leech antihemostatic proteins share the T-knot scaffold, a disulfide-reinforced structural motif. Biological Chemistry, 379(11), 1387-1389.