Analysis of the tertiary structure of protein β-sheet sandwiches

摘要: Abstract The face to stacking of two primarily antiparallel β-sheets form a β-sandwich occurs in several globular proteins including the domains immunoglobulins. We have examined tertiary structures ten β-sandwiches show that they well-defined structural class with following features. 1. (1) A standard packing geometry twisted separated by 8.3 10.3 and rotated anticlockwise 20 ° 50 °. 2. (2) Common values positions for changes solvent accessible contact area during condensation β-strands → β-sandwich. In particular sheet produces anti-complementary patterns changes. 3. (3) sheet-sheet interface has bilayer structure when medium sized residues sheets stack but there is interdigitation large small different sheets. 4. (4) nature β-sheet explains both left-handed rotation between observed pattern These observations been incorporated into computer algorithm predict fold from primary secondary structure.