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Copyright © 2007 by Karl Oberholser,
Messiah College, Grantham, PA USA.

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Coiled-coil Motif

A coiled-coil or superhelix is formed by coiling two, three or four a helices together. The helical strands are held together by the hydrophobic force formed between nonpolar side chains from the different peptide strands. A heptad repeat pattern of hydrophobic residues in the primary structure consistently bring these nonpolar side chains together every seventh residue. These nonpolar residues from different strands are properly located to interact with one another because the helix is slightly distorted by being less tightly wound than the normal a helix so that it has a pitch of 0.51 instead of 0.54 and there are 3.5 residues per turn instead of 3.6. With this slight left-handed twist to the right-handed a helix, there are exactly seven residues per two turns (2 x 3.5) in the distorted a helix, and therefore the side chains of the heptad residues are in place to interact with each other. (1)

This series of slides illustrates how the side chains of the heptad repeats align and gives examples of the coiled-coil motif.

Reference
1. Biochemistry, 3rd ed., R. H. Garrett & C. M. Grisham, Thomson/Brooks/Cole, page 181.

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Two Coiled Strands
GCN4 protein

Observe the slight coil in the strands.
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Two Coiled Strands
Heptad Repeat

Every seventh residue, shown in spacefill, in a chain is nonpolar, and with 3.5 residues per turn each heptad repeat is aligned with the one below and above it, as well as being in position to interact with the heptad repeat on a second strand.
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Two Coiled Strands
Looking down the spline of contact.
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Two Coiled Strands
The side chains of the residues located between the heptad repeats spiral around the helix away from the side chains on the partner strand, thus not permitting interactions between these side chains of the two strands.
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Three Coiled Strands
Influenza Hemagglutinin - one of the viral proteins that is immunologically active

There are three peptide strands that form the coiled-coil.
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Three Coiled Strands
The heptrad repeats of each strand are shown in spacefill.
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Coiled-Coils in Globular Protein
Catabolite Activator Protein (CAP) - a globular protein that is an important regulator of several aspects of catabolism

Notice the two coiled a helices in the center of the structure. Each coil is a part of a different subunit, and the formation of the coiled-coil plays a pivotal role in holding the two subunits together.
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Coiled-Coils in Globular Proteins
CAP

The heptrad repeats are shown in spacefill.
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