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A conserved trimerization motif controls the topology of short coiled coils
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 156430
Author(s) Kammerer, R. A.; Kostrewa, D.; Progias, P.; Honnappa, S.; Avila, D.; Lustig, A.; Winkler, F. K.; Pieters, J.; Steinmetz, M. O.
Author(s) at UniBasel Pieters, Jean
Year 2005
Title A conserved trimerization motif controls the topology of short coiled coils
Journal Proceedings of the National Academy of Sciences of the United States of America
Volume 102
Number 39
Pages / Article-Number 13891-13896
Keywords protein engineering, sequence-to-structure rules, protein-protein interaction, salt bridges, x-ray crystallography
Abstract In recent years, short coiled coils have been used for applications ranging from biomaterial to medical sciences. For many of these applications knowledge of the factors that control the topology of the engineered protein systems is essential. Here, we demonstrate that trimerization of short coiled coils is determined by a distinct structural motif that encompasses specific networks of surface salt bridges and optimal hydrophobic packing interactions. The motif is conserved among intracellular, extracellular, viral, and synthetic proteins and defines a universal molecular determinant for trimer formation of short coiled coils. In addition to being of particular interest for the biotechnological production of candidate therapeutic proteins, these findings may be of interest for viral drug development strategies.
Publisher National Academy of Sciences
ISSN/ISBN 0027-8424
edoc-URL http://edoc.unibas.ch/dok/A5259403
Full Text on edoc Restricted
Digital Object Identifier DOI 10.1073/pnas.0502390102
ISI-Number WOS:000232231900034
Document type (ISI) Article
 
   

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