Crystal structure of the signal sequence binding subunit of the signal recognition particle.

Article Details

Citation

Keenan RJ, Freymann DM, Walter P, Stroud RM

Crystal structure of the signal sequence binding subunit of the signal recognition particle.

Cell. 1998 Jul 24;94(2):181-91.

PubMed ID
9695947 [ View in PubMed
]
Abstract

The crystal structure of the signal sequence binding subunit of the signal recognition particle (SRP) from Thermus aquaticus reveals a deep groove bounded by a flexible loop and lined with side chains of conserved hydrophobic residues. The groove defines a flexible, hydrophobic environment that is likely to contribute to the structural plasticity necessary for SRP to bind signal sequences of different lengths and amino acid sequence. The structure also reveals a helix-turn-helix motif containing an arginine-rich alpha helix that is required for binding to SRP RNA and is implicated in forming the core of an extended RNA binding surface.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Signal recognition particle proteinO07347Details