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Beta-sandwich or β-sandwich domains consisting of 80 to 350 amino acids occur commonly in proteins. They are characterized by two opposing antiparallel beta sheets (β-sheets). [ 1 ] The number of strands found in such domains may differ from one protein to another. β-sandwich domains are subdivided in a variety of different folds.
Explanation of all-beta topologies: "orthogonal beta-sandwiches" are beta-barrels (as defined in this article); "aligned" beta-sandwiches" correspond to beta-sandwich folds in SCOP classification. all-beta folds in SCOP database (folds 54 to 100 are water-soluble beta-barrels).
This domain has a 3-layer structure, and contains a beta-sandwich fold of unusual topology, and contains a putative tRNA-binding structural motif. [2] In Thermus thermophilus, both the catalytic alpha- and the non-catalytic beta-subunits comprise the characteristic fold of the class II active-site domains.
The jelly roll or Swiss roll fold is a protein fold or supersecondary structure composed of eight beta strands arranged in two four-stranded sheets. The name of the structure was introduced by Jane S. Richardson in 1981, reflecting its resemblance to the jelly or Swiss roll cake. [ 2 ]
The Rossmann fold is a tertiary fold found in proteins that bind nucleotides, such as enzyme cofactors FAD, NAD +, and NADP +.This fold is composed of alternating beta strands and alpha helical segments where the beta strands are hydrogen bonded to each other forming an extended beta sheet and the alpha helices surround both faces of the sheet to produce a three-layered sandwich.
PDB_1jk8_EBI.jpg (800 × 600 pixels, file size: 40 KB, MIME type: image/jpeg) ... • Fold: Immunoglobulin-like beta-sandwich • Superfamily: Immunoglobulin
The immunoglobulin domain, also known as the immunoglobulin fold, is a type of protein domain that consists of a 2-layer sandwich of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek key topology, [1] [2] consisting of about 125 amino acids. The backbone switches repeatedly between the two β-sheets.
PKD (Polycystic Kidney Disease) domain was first identified in the polycystic kidney disease protein, polycystin-1 (PKD1 gene), and contains an Ig-like fold consisting of a beta-sandwich of seven strands in two sheets with a Greek key topology, although some members have additional strands. [1]