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A conserved trimerization motif controls the topology of short coiled coils

Kammerer, R. A. and Kostrewa, D. and Progias, P. and Honnappa, S. and Avila, D. and Lustig, A. and Winkler, F. K. and Pieters, J. and Steinmetz, M. O.. (2005) A conserved trimerization motif controls the topology of short coiled coils. Proceedings of the National Academy of Sciences of the United States of America, 102 (39). pp. 13891-13896.

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Infection Biology > Biochemistry (Pieters)
UniBasel Contributors:Pieters, Jean
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:National Academy of Sciences
ISSN:0027-8424
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
Identification Number:
Last Modified:26 Sep 2017 07:42
Deposited On:22 Mar 2012 13:22

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