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

Citation
P. Ascenzi et al., Leech antihemostatic proteins share the T-knot scaffold, a disulfide-reinforced structural motif, BIOL CHEM, 379(11), 1998, pp. 1387-1389
Citations number
6
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOLOGICAL CHEMISTRY
ISSN journal
14316730 → ACNP
Volume
379
Issue
11
Year of publication
1998
Pages
1387 - 1389
Database
ISI
SICI code
1431-6730(199811)379:11<1387:LAPSTT>2.0.ZU;2-O
Abstract
The occcurence of similar topologies among unrelated proteins is an emergin g theme in structural biology. Here we report that the T-knot scaffold, a d isulfide-reinforced structural motif shared by knottins and EGF-like protei ns, is also present in leech antihemostatic proteins. Our finding emphasize s the versatile nature of this small structural motif, representing a compa ct structural unit suitable for the diverse biological functions performed by knottins, EGF-like proteins and leech antihemostatic proteins.