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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 ...
When a sequence motif appears in the exon of a gene, it may encode the "structural motif" of a protein; that is a stereotypical element of the overall structure of the protein. Nevertheless, motifs need not be associated with a distinctive secondary structure.
The Walker A and Walker B motifs are protein sequence motifs, known to have highly conserved three-dimensional structures. These were first reported in ATP-binding proteins by Walker and co-workers in 1982. [1] Of the two motifs, the A motif is the main "P-loop" responsible for binding phosphate, while the B motif is a much less conserved ...
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. Structural domain [ edit ]
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.
Similar motifs occur with serine or threonine as residue i, which are called ST turns. [13] In spite of serine and threonine having one less sidechain atom, such that the sidechain-mainchain mimicry of β turns is imperfect, these features occur in proteins as the four types in numbers approaching those of Asx turns.
Originally discovered in bacteria, the helix-turn-helix motif is commonly found in repressor proteins and is about 20 amino acids long. In eukaryotes, the homeodomain comprises 2 helices, one of which recognizes the DNA (aka recognition helix). They are common in proteins that regulate developmental processes. [5]