Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.
Proc Natl Acad Sci U S A
; 102(40): 14278-83, 2005 Oct 04.
Article
em En
| MEDLINE
| ID: mdl-16179394
ABSTRACT
We have observed a common sequence motif in membrane proteins, which we call a glycine zipper. Glycine zipper motifs are strongly overrepresented and conserved in membrane protein sequences, and mutations in glycine zipper motifs are deleterious to function in many cases. The glycine zipper has a significant structural impact, engendering a strong driving force for right-handed packing against a neighboring helix. Thus, the presence of a glycine zipper motif leads directly to testable structural hypotheses, particularly for a subclass of glycine zipper proteins that form channels. For example, we suggest that the membrane pores formed by the amyloid-beta peptide in vitro are constructed by glycine zipper packing and find that mutations in the glycine zipper motif block channel formation. Our findings highlight an important structural motif in a wide variety of normal and pathological processes.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Modelos Moleculares
/
Motivos de Aminoácidos
/
Glicina
/
Canais Iônicos
/
Proteínas de Membrana
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Ano de publicação:
2005
Tipo de documento:
Article