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

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 journal › Article › peer-review

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 language	English
Pages (from-to)	1387-1389
Number of pages	3
Journal	Biological Chemistry
Volume	379
Issue number	11
Publication status	Published - 1998

Keywords

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

ASJC Scopus subject areas

Biochemistry

Cite this

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

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.",

keywords = "Antistasin, Decorsin, EGF-like proteins, Hirudin, Knottins, T-knot scaffold",

author = "Paolo Ascenzi and Martino Bolognesi and Daniele Catalucci and Stefano Pascarella and Margherita Ruoppolo and Menico Rizzi",

year = "1998",

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pages = "1387--1389",

journal = "Biological Chemistry",

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TY - JOUR

T1 - Leech antihemostatic proteins share the T-knot scaffold, a disulfide-reinforced structural motif

AU - Ascenzi, Paolo

AU - Bolognesi, Martino

AU - Catalucci, Daniele

AU - Pascarella, Stefano

AU - Ruoppolo, Margherita

AU - Rizzi, Menico

PY - 1998

Y1 - 1998

N2 - 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.

AB - 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.

KW - Antistasin

KW - Decorsin

KW - EGF-like proteins

KW - Hirudin

KW - Knottins

KW - T-knot scaffold

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M3 - Article

C2 - 9865615

AN - SCOPUS:0031764172

VL - 379

SP - 1387

EP - 1389

JO - Biological Chemistry

JF - Biological Chemistry

SN - 1431-6730

IS - 11

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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