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Meeting Abstract

Hexads and nonads specify a new type of coiled-coil fiber

MPS-Authors
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Hartmann,  MD       
Molecular Recognition and Catalysis Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Hernandez Alvarez,  B       
Conservation of Protein Structure and Function Group, Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Bassler,  J
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Lupas,  AN       
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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http://www.ngp-net.gmc.vu.lt/wp-content/uploads/2018/10/NGP-Net4_abstract_book.pdf
(Abstract)

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Citation

Hartmann, M., Hernandez Alvarez, B., Bassler, J., & Lupas, A. (2018). Hexads and nonads specify a new type of coiled-coil fiber. In 4th Symposium on Non-Globular Proteins (NGP-NET 2018) (pp. 24).


Cite as: https://hdl.handle.net/21.11116/0000-000E-0EDB-D
Abstract
Coiled coils are formed by α-helices winding around each other into superhelical bundles [1,2]. They are characterized by a specific geometry of interaction, called knobs-into-holes, in which core residues contributed by alternating segments of 3 and 4 residues mesh regularly along a seam that runs the length of the helices. This alternation yields a periodicity of 7 residues over 2 helical turns – the heptad repeat – but variant coiled coils can be formed by other periodicities resulting from the combination of 3- and 4-residue segments, such as decads (3+4+3), hendecads (3+4+4), or pentadecads (3+4+4+4), but not with consecutive segments of 3 residues (3+3 or 3+3+3).