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An autonomous folding unit mediates the assembly of two-stranded coiled coils.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Landwehr, R. Aebi, U. Lustig, A. Kammerer, R. A. Steinmetz, M. O. Schulthess, T. Engel, J.
Description	Author Affiliation: Kammerer RA ( Department of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.);
Abstract	Subunit oligomerization of many proteins is mediated by coiled-coil domains. Although the basic features contributing to the thermodynamic stability of coiled coils are well understood, the mechanistic details of their assembly have not yet been dissected. Here we report a 13-residue sequence pattern that occurs with limited sequence variations in many two-stranded coiled coils and that is absolutely required for the assembly of the Dictyostelium discoideum actin-bundling protein cortexillin I and the yeast transcriptional activator GCN4. The functional relationship between coiled-coil 'trigger' sequences was manifested by replacing the intrinsic trigger motif of GCN4 with the related sequence from cortexillin I. We demonstrate that these trigger sequences represent autonomous helical folding units that, in contrast to arbitrarily chosen heptad repeats, can mediate coiled-coil formation. Aside from being of general interest for protein folding, trigger motifs should be of particular importance in the protein de novo design.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	95
Language	English
Publisher	National Academy of Sciences
Publisher Date	1998-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	DNA-Binding Proteins Dictyostelium Chemistry Fungal Proteins Microfilament Proteins Protein Folding Protein Kinases Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Amino Acid Sequence Animals Metabolism Molecular Sequence Data Protozoan Proteins Sequence Analysis Trans-Activators Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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