All-β proteins

From Wikipedia, the free encyclopedia

An all-β proteins is a class of structural domains in which the secondary structure is composed entirely of β-sheets, with the possible exception of a few isolated α-helices on the periphery.

Common examples include the SH3 domain, the beta-propeller domain, the immunoglobulin fold and B3 DNA binding domain.

[edit] See also

• SCOP database
• CATH database
• FSSP database

v • d • e Protein tertiary structure General Structural domain | Protein folding | Structure determination methods All-α folds: Helix bundle | Globin fold | Homeodomain fold | Alpha solenoid All-β folds: Immunoglobulin fold | Beta barrel | Beta-propeller α/β folds: TIM barrel | Leucine-rich repeat | Flavodoxin fold | Rossmann fold | Thioredoxin fold | Trefoil knot fold α+β folds: DNA clamp | Ferredoxin fold | Ribonuclease A | SH2-like fold Irregular folds: Conotoxin ←Secondary structure Quaternary structure→