Protein design by fusion: implications for protein structure prediction and evolution.
Acta Crystallogr D Biol Crystallogr
; 69(Pt 12): 2451-60, 2013 Dec.
Article
em En
| MEDLINE
| ID: mdl-24311586
ABSTRACT
Domain fusion is a useful tool in protein design. Here, the structure of a fusion of the heterodimeric flagella-assembly proteins FliS and FliC is reported. Although the ability of the fusion protein to maintain the structure of the heterodimer may be apparent, threading-based structural predictions do not properly fuse the heterodimer. Additional examples of naturally occurring heterodimers that are homologous to full-length proteins were identified. These examples highlight that the designed protein was engineered by the same tools as used in the natural evolution of proteins and that heterodimeric structures contain a wealth of information, currently unused, that can improve structural predictions.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Plantas
/
Aquifoliaceae
Tipo de estudo:
Prognostic_studies
/
Risk_factors_studies
Idioma:
En
Revista:
Acta Crystallogr D Biol Crystallogr
Ano de publicação:
2013
Tipo de documento:
Article