Analysis of the crystal structure of a parallel three‐stranded coiled coil

Author:

de March Matteo12ORCID,Hickey Neal1,Geremia Silvano1ORCID

Affiliation:

1. Department of Chemical and Pharmaceutical Sciences University of Trieste Trieste Italy

2. Laboratory for Environmental and Life Sciences University of Nova Gorica Nova Gorica Slovenia

Abstract

AbstractHere, we present the crystal structure of the synthetic peptide KE1, which contains four K‐coil heptads separated in the middle by the QFLMLMF heptad. The structure determination reveals the presence of a canonical parallel three stranded coiled coil. The geometric characteristics of this structure are compared with other coiled coils with the same topology. Furthermore, for this topology, the analysis of the propensity of the single amino acid to occupy a specific position in the heptad sequence is reported. A number of viral proteins use specialized coiled coil tail needles to inject their genetic material into the host cells. The simplicity and regularity of the coiled coil arrangement made it an attractive system for de novo design of key molecules in drug delivery systems, vaccines, and therapeutics.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

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