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Increase of functional diversity by alternative splicing

Official URL:https://doi.org/10.1016/S0168-9525(03)00023-4
PubMed:View item in PubMed
Creators Name:Kriventseva, E.V. and Koch, I. and Apweiler, R. and Vingron, M. and Bork, P. and Gelfand, M.S. and Sunyaev, S.
Journal Title:Trends in Genetics
Journal Abbreviation:Trends Genet
Volume:19
Number:3
Page Range:124-128
Date:March 2003
Keywords:Alternative Splicing, Amino Acid Sequence, Amino Acids, Computational Biology, Molecular Models, Protein Databases, Protein Isoforms, Tertiary Protein Structure, Selection, Animals
Abstract:A large-scale analysis of protein isoforms arising from alternative splicing shows that alternative splicing tends to insert or delete complete protein domains more frequently than expected by chance, whereas disruption of domains and other structural modules is less frequent. If domain regions are disrupted, the functional effect, as predicted from 3D structure, is frequently equivalent to removal of the entire domain. Also, short alternative splicing events within domains, which might preserve folded structure, target functional residues more frequently than expected. Thus, it seems that positive selection has had a major role in the evolution of alternative splicing.
ISSN:0168-9525
Publisher:Elsevier (The Netherlands)
Item Type:Article

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