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 |
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Keywords
- Antistasin
- Decorsin
- EGF-like proteins
- Hirudin
- Knottins
- T-knot scaffold
ASJC Scopus subject areas
- Biochemistry
Cite this
Leech antihemostatic proteins share the T-knot scaffold, a disulfide-reinforced structural motif. / Ascenzi, Paolo; Bolognesi, Martino; Catalucci, Daniele; Pascarella, Stefano; Ruoppolo, Margherita; Rizzi, Menico.
In: Biological Chemistry, Vol. 379, No. 11, 1998, p. 1387-1389.Research output: Contribution to journal › Article
}
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
UR - http://www.scopus.com/inward/record.url?scp=0031764172&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0031764172&partnerID=8YFLogxK
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 -