The N-terminal to C-terminal motif in protein folding and function
AUTOR(ES)
Krishna, Mallela M. G.
FONTE
National Academy of Sciences
RESUMO
Essentially all proteins known to fold kinetically in a two-state manner have their N- and C-terminal secondary structural elements in contact, and the terminal elements often dock as part of the experimentally measurable initial folding step. Conversely, all N–C no-contact proteins studied so far fold by non-two-state kinetics. By comparison, about half of the single domain proteins in the Protein Data Bank have their N- and C-terminal elements in contact, more than expected on a random probability basis but not nearly enough to account for the bias in protein folding. Possible reasons for this bias relate to the mechanisms for initial protein folding, native state stability, and final turnover.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=545867Documentos Relacionados
- The mouse c-rel protein has an N-terminal regulatory domain and a C-terminal transcriptional transactivation domain.
- Both N- and C-terminal domains of RelB are required for full transactivation: role of the N-terminal leucine zipper-like motif.
- Properties of Rab5 N-terminal domain dictate prenylation of C-terminal cysteines.
- Differential detection of type II collagen N-terminal and C-terminal denaturation epitopes in degrading cartilage.
- Siah-1 N-Terminal RING Domain Is Required for Proteolysis Function, and C-Terminal Sequences Regulate Oligomerization and Binding to Target Proteins