A hinge region cis-proline in ribonuclease A acts as a conformational gatekeeper for C-terminal domain swapping.

ABSTRACT: Domain swapping, the process in which a structural unit is exchanged between monomers to create a dimer containing two subunits of the monomeric fold, is believed to be an important mechanism for oligomerization and the formation of amyloid fibrils. Structural studies have implicated proline as an important residue for domain swapping due to its increased frequency in hinge regions preceding swapped arms. We hypothesized that proline's unique ability to populate both cis and trans peptide bond conformations may allow proline to act as a conformational gatekeeper, regulating interconversion between monomer and domain-swapped dimer forms. The hinge region of RNase A contains a proline at residue 114 that adopts a cis conformation in the monomer and extends to a trans conformation in the C-te

SUBMITTER: Miller KH 

PROVIDER: S-EPMC2911975 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature