Identifying polymer-forming SAM domains.
Proteins
; 74(1): 1-5, 2009 Jan.
Article
en En
| MEDLINE
| ID: mdl-18831011
ABSTRACT
Sterile alpha motif (SAM) domains are common protein modules in eukaryotic cells. It has not been possible to assign functions to uncharacterized SAM domains because they have been found to participate in diverse functions ranging from protein-protein interactions to RNA binding. Here we computationally identify likely members of the subclass of SAM domains that form polymers. Sequences were virtually threaded onto known polymer structures and then evaluated for compatibility with the polymer. We find that known SAM polymers score better than the vast majority of known nonpolymers 100% (7 of 7) of known polymers and only 8% of known nonpolymers (1 of 12) score above a defined threshold value. Of 2901 SAM family members, we find 694 that score above the threshold and are likely polymers, including SAM domains from the proteins Lethal Malignant Brain Tumor, Bicaudal-C, Liprin-beta, Adenylate Cyclase, and Atherin.
Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Polímeros
/
Algoritmos
/
Proteínas
/
Secuencias de Aminoácidos
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Proteins
Asunto de la revista:
BIOQUIMICA
Año:
2009
Tipo del documento:
Article