Interactions crucial for three-dimensional domain swapping in the HP-RNase variant PM8.

ABSTRACT: The structural determinants that are responsible for the formation of higher order associations of folded proteins remain unknown. We have investigated the role on the dimerization process of different residues of a domain-swapped dimer human pancreatic ribonuclease variant. This variant is a good model to study the dimerization and swapping processes because dimer and monomer forms interconvert, are easily isolated, and only one dimeric species is produced. Thus, simple models for the swapping process can be proposed. The dimerization (dissociation constant) and swapping propensity have been studied using different variants with changes in residues that belong to different putative molecular determinants of dimerization. Using NMR spectroscopy, we show that these mutations do not substant

SUBMITTER: Tubert P 

PROVIDER: S-EPMC3136784 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature