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The heptad repeat is an example of a structural motif that consists of a repeating pattern of seven amino acids: [1]. a b c d e f g H P P H C P C . where H represents ...
Coiled coils usually contain a repeated pattern, hxxhcxc, of hydrophobic (h) and charged (c) amino-acid residues, referred to as a heptad repeat. [10] The positions in the heptad repeat are usually labeled abcdefg, where a and d are the hydrophobic positions, often being occupied by isoleucine, leucine, or valine.
Heptad ('group of 7') or heptade may refer to: Heptad (chord), heptachord in music (set) Heptad (computing), a group of 7 bits in computing; Heptad repeat, a structural motif in proteins; L'Heptade, an album by Harmonium in 1976
In the case of leucine zippers, leucines are predominant at the d position of the heptad repeat. These residues pack against each other every second turn of the alpha-helices, and the hydrophobic region between two helices is completed by residues at the a positions, which are also frequently hydrophobic.
The MFN2 comprises a large cytosolic GTPase domain at the N-terminal, followed by a coiled-coil heptad-repeat (HR1) domain, a proline-rich (PR) region, two sequential transmembrane (TM) domains crossing the OMM and a second cytosolic heptad-repeat (HR2) domain at the C-terminal.
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Gp41 has three prominent regions within the sequence: the ectodomain, the transmembrane domain, and the cytoplasmic domain. The ectodomain, which comprises residues 511-684, can be further broken down into the fusion peptide region (residues 512-527), the helical N-terminal heptad repeat (NHR) and C-terminal heptad repeat (CHR).
The KRAB domain had initially been identified in 1988 as a periodic array of leucine residues separated by six amino acids 5’ to the zinc finger region of KOX1/ZNF10 [7] coined heptad repeat of leucines (also known as a leucine zipper). [8] Later, this domain was named in association with the C2H2-Zinc finger proteins Krüppel associated box ...