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An individual motif usually consists of only a few elements, e.g., the 'helix-turn-helix' motif which has just three. Note that, while the spatial sequence of elements may be identical in all instances of a motif, they may be encoded in any order within the underlying gene. In addition to secondary structural elements, protein structural motifs ...
Proteins are frequently described as consisting of several structural units. These units include domains, motifs, and folds. Despite the fact that there are about 100,000 different proteins expressed in eukaryotic systems, there are many fewer different domains, structural motifs and folds.
2009: Grove, De Masi et al., identified novel short DNA motifs, bound by a subset of bHLH proteins, which they defined as "E-box-like sequences". These are in the form of CAYRMK, where Y stands for C or T, R is A or G, M is A or C and K is G or T. [ 16 ]
Sequence motif, a sequence pattern of nucleotides in a DNA sequence or amino acids in a protein; Short linear motif, a stretch of protein sequence that mediates protein–protein interaction; Structural motif, a pattern in a protein structure formed by the spatial arrangement of amino acids
Pages in category "Protein structural motifs" The following 56 pages are in this category, out of 56 total. This list may not reflect recent changes. 0–9.
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.
In the area of protein structural motifs, niches are three or four amino acid residue features in which main-chain CO groups are bridged by positively charged or δ + groups. [1] [2] [3] The δ + groups include groups with two hydrogen bond donor atoms such as NH 2 groups and water molecules.
Schellman loops incorporate a three amino acid residue RL nest (protein structural motif), [12] [13] in which three mainchain NH groups (from Schellman loop residues i+3 to i+5) form a concavity for hydrogen bonding to carbonyl oxygens. About 2.5% of amino acids in proteins belong to Schellman loops.