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Trends Biochem Sci. 2017 Feb;42(2):130-140. doi: 10.1016/j.tibs.2016.10.007. Epub 2016 Nov 21.

Coiled Coils - A Model System for the 21st Century.

Author information

1
Department of Protein Evolution, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany. Electronic address: andrei.lupas@tuebingen.mpg.de.
2
Department of Protein Evolution, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany.

Abstract

α-Helical coiled coils were described more than 60 years ago as simple, repetitive structures mediating oligomerization and mechanical stability. Over the past 20 years, however, they have emerged as one of the most diverse protein folds in nature, enabling many biological functions beyond mechanical rigidity, such as membrane fusion, signal transduction, and solute transport. Despite this great diversity, their structures can be described by parametric equations, making them uniquely suited for rational protein design. Far from having been exhausted as a source of structural insight and a basis for functional engineering, coiled coils are poised to become even more important for protein science in the coming decades.

KEYWORDS:

coiled coil; diversity; protein design; structure

PMID:
27884598
DOI:
10.1016/j.tibs.2016.10.007
[Indexed for MEDLINE]

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