A conserved trimerization motif controls the topology of short coiled coils

Richard A. Kammerer, Dirk Kostrewa, Pavlos Progias, Srinivas Honnappa, David Avila, Ariel Lustig, Fritz K. Winkler, Jean Pieters, Michel O. Steinmetz

    Research output: Contribution to journalArticlepeer-review

    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. © 2005 by The National Academy of Sciences of the USA.
    Original languageEnglish
    Pages (from-to)13891-13896
    Number of pages5
    JournalProceedings of the National Academy of Sciences of the United States of America
    Volume102
    Issue number39
    DOIs
    Publication statusPublished - 27 Sept 2005

    Keywords

    • Protein engineering
    • Protein-protein interaction
    • Salt bridges
    • Sequence-to-structure rules
    • X-ray crystallography

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