PMID:15189152
| Citation |
Doudna, JA and Batey, RT (2004) Structural insights into the signal recognition particle. Annu. Rev. Biochem. 73:539-57 |
|---|---|
| Abstract |
The signal recognition particle (SRP) directs integral membrane and secretory proteins to the cellular protein translocation machinery during translation. The SRP is an evolutionarily conserved RNA-protein complex whose activities are regulated by GTP hydrolysis. Recent structural investigations of SRP functional domains and interactions provide new insights into the mechanisms of SRP activity in all cells, leading toward a comprehensive understanding of protein trafficking by this elegant pathway. |
| Links |
PubMed Online version:10.1146/annurev.biochem.73.011303.074048 |
| Keywords |
Animals; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Guanosine Triphosphate/metabolism; Models, Biological; Models, Molecular; Molecular Structure; Phylogeny; Protein Biosynthesis; Protein Conformation; Receptors, Cytoplasmic and Nuclear/chemistry; Receptors, Cytoplasmic and Nuclear/genetics; Receptors, Cytoplasmic and Nuclear/metabolism; Ribosomes/metabolism; Signal Recognition Particle/chemistry; Signal Recognition Particle/genetics; Signal Recognition Particle/metabolism |
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