Chen C.K.-M.NEI-LI CHANWang A.H.-J.2020-02-062020-02-0620110968-0004https://www.scopus.com/inward/record.uri?eid=2-s2.0-80053338227&doi=10.1016%2fj.tibs.2011.07.004&partnerID=40&md5=1e6823949bec6c43bafdb2666d20a7b3https://scholars.lib.ntu.edu.tw/handle/123456789/454017The β-propeller is a highly symmetrical structure with 4-10 repeats of a four-stranded antiparallel β-sheet motif. Although β-propeller proteins with different blade numbers all adopt disc-like shapes, they are involved in a diverse set of functions, and defects in this family of proteins have been associated with human diseases. However, it has remained ambiguous how variations in blade number could alter the function of β-propellers. In addition to the regularly arranged β-propeller topology, a recently discovered β-pinwheel propeller has been found. Here, we review the structural and functional diversity of β-propeller proteins, including β-pinwheels, as well as recent advances in the typical and atypical propeller structures. ? 2011 Elsevier Ltd.[SDGs]SDG3aryldialkylphosphatase 1; beta propeller protein; hemopexin; matrix metalloproteinase; membrane protein; neurotrophin receptor; sortilin; unclassified drug; alpha helix; Alzheimer disease; beta pinwheel; beta sheet; DNA binding; DNA binding domain; Glanzmann disease; human; nonhuman; priority journal; protein domain; protein folding; protein function; protein motif; protein protein interaction; protein structure; retina degeneration; review; structure activity relation; Amino Acid Sequence; Animals; Conserved Sequence; Enzymes; Humans; Intracellular Signaling Peptides and Proteins; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiaryreview10.1016/j.tibs.2011.07.0042-s2.0-80053338227