Determinants of stability for the E6 protein of papillomavirus type 16.

ABSTRACT: E6 is an oncoprotein produced by human papillomavirus (HPV). The E6 protein from high-risk HPV type 16 contains two zinc-binding domains with two C-x-x-C motifs each. E6 exerts its transforming functions through formation of a complex with E6AP, which binds p53 and stimulates its degradation. There have been few biophysical and structural studies due to difficulty in preparation of soluble protein; here we describe the preparation of soluble E6 constructs including the two separated zinc-binding domains of E6. These proteins are used to examine the extent to which the two domains cooperate to mediate E6 function, how zinc influences the behavior of E6 protein, and which domains mediate aggregation. We demonstrate, using p53 degradation, E6AP binding, and hDlg (human homolog of the Drosophi

SUBMITTER: Liu Y 

PROVIDER: S-EPMC2768073 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature