N-terminal extension of beta B1-crystallin: identification of a critical region that modulates protein interaction with beta A3-crystallin.

ABSTRACT: The human lens proteins beta-crystallins are subdivided into acidic (betaA1-betaA4) and basic (betaB1-betaB3) subunit groups. These structural proteins exist at extremely high concentrations and associate into oligomers under physiological conditions. Crystallin acidic-basic pairs tend to form strong heteromolecular associations. The long N-terminal extensions of beta-crystallins may influence both homo- and heteromolecular interactions. However, identification of the critical regions of the extensions mediating protein associations has not been previously addressed. This was studied by comparing the self-association and heteromolecular associations of wild-type recombinant betaA3- and betaB1-crystallins and their N-terminally truncated counterparts (betaA3DeltaN30 and betaB1DeltaN56) usin

SUBMITTER: Dolinska MB 

PROVIDER: S-EPMC2764403 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature