Coiled coil - Wikipedia
A coiled coil is a structural motif in proteins in which 2–7 [1] alpha-helices are coiled together like the strands of a rope. (Dimers and trimers are the most common types.) They have been found in roughly 5-10% of proteins and have a variety of functions. [2] . They are one of the most widespread motifs found in protein-protein interactions.
Coiled‐coils: The long and short of it - PMC - PubMed Central …
Coiled‐coil domains vary in length from the short to the extremely long, and from being almost invariant in sequence to hypervariable. Some coiled‐coils appear to function simply as molecular spacers while others have evolved the capacity to communicate conformational changes along …
The Structure and Topology of α-Helical Coiled Coils - PMC
Jan 19, 2017 · Coiled coil structures with different periodicities. Top row: The left-handed supercoil of GCN4-pII (PDB: 1GCM) with a periodicity of seven residues over two helical turns (7/2), the straight helices of tetrabrachion (PDB: 1FE6) with 11/3 periodicity, and the right-handed supercoil of human VASP (PDB: 1USD) with 15/4 periodicity.
The physics, chemistry, and biology of α-helical coiled coils
Jan 3, 2023 · For coiled-coil research, new challenges include the following: achieving fully quantitative (free-energy) predictions for coiled-coil structure, stability, and partner selection; gaining a deeper understanding of coiled-coil dynamics and plasticity and how this relates to coiled-coil function.
Functional and Structural Roles of Coiled Coils | SpringerLink
Jan 19, 2017 · A major hallmark of coiled coils is their structural simplicity: they consist of two or more α-helices that are wound around each other into supercoils with a common hydrophobic core, while the packing of the helices and the side-chains in the core satisfies simple rules.
The physics, chemistry, and biology of α-helical coiled coils
Apr 1, 2023 · This perspective presents our current understanding of one class of protein assembly, the α-helical coiled coils. At first sight, these are straightforward: sequence repeats of hydrophobic (h) and polar (p) residues, (hpphppp)n, direct the folding and assembly of amphipathic α helices into bundles.
Coiled coils: a highly versatile protein folding motif
Feb 1, 2001 · The acidic extension forms a coiled-coil structure with the VBP basic region to form an A-VBP–VBP heterodimer. This new α-helical structure extends the leucine zipper N-terminally, stabilizing the complex by 2.0 kcal mol −1, and consequently A …
α/β coiled coils - eLife
Jan 15, 2016 · Coiled coils are the best-understood protein fold, as their backbone structure can uniquely be described by parametric equations. This level of understanding has allowed their manipulation in unprecedented detail.
The myosin coiled-coil is a truly elastic protein structure
Nov 24, 2002 · The coiled-coil undergoes a massive structural transition at forces between 20 and 25 pN where the coil extends to about 2.5 times its original length. Unlike all other proteins investigated...
The design of coiled-coil structures and assemblies - PubMed
This review summarizes the current design rules for coiled coils, and describes some of the key successful coiled-coil designs that have been created to date.