Sequence determinants of function and evolution in serine proteases

Citation
Mm. Krem et al., Sequence determinants of function and evolution in serine proteases, TREND CARD, 10(4), 2000, pp. 171-176
Citations number
52
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Cardiovascular & Hematology Research
Journal title
TRENDS IN CARDIOVASCULAR MEDICINE
ISSN journal
1050-1738 → ACNP
Volume
10
Issue
4
Year of publication
2000
Pages
171 - 176
Database
ISI
SICI code
1050-1738(200005)10:4<171:SDOFAE>2.0.ZU;2-J
Abstract
Serine proteases of the chymotrypsin family have maintained a common fold o ver an evolutionary span of more than one billion years. Notwithstanding mo dest changes in sequence, this class of enzymes has developed a wide variet y of substrate specificities and important biological functions such as fib rinolysis, blood coagulation, and complement activation. Recently it has be come apparent that the protease domain, especially its C-terminal sequence, accounts fully for this functional diversity and is the most important ele ment in shaping serine protease evolution. (Trends Cardiovasc Med 2000; 10: 171-176). (C) 2001, Elsevier Science Inc. All rights reserved.