Last modified 5th.July '95
Back to main PPS Index
Back to Tertiary Structure Index
DOMAIN MOVEMENTS
This section is largely based on the excellent review by
Gerstein et al. (1994). Mark Gerstein is also largely responsible for
The Protein Motions Database
Protein flexibility is demonstrated by large relative movements of
domains, for example, in aspartic proteinases the two lobes have large
relative shifts as identified by Sali et al., (1992).
Such motions are important for functions like catalysis,
ligand binding, regulation of activity, formation of protein
assemblies and transport of metabolites. Often the domains constitute
a binding site at the interface wherein closed conformations of
domains correspond to inactive form of the enzyme while open
conformations of domains correspond to the active form of the
enzyme, illustrating induced fit in recognition (Koshland, 1958).
Mechansisms of domain movements -