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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.