SRP--Where the RNA and Membrane Worlds Meet
- 18 February 2000
- journal article
- perspective
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 287 (5456), 1212-1213
- https://doi.org/10.1126/science.287.5456.1212
Abstract
Working out how the signal recognition particle (SRP) of cells directs newly synthesized proteins destined for secretion to the endoplasmic reticulum (ER) has proved a gargantuan task. That task has just been made easier, as explained in a Perspective by Peter Walter and colleagues, by the solving of the crystal structure of the RNA-protein core of the SRP ( Batey et al.)Keywords
This publication has 10 references indexed in Scilit:
- Crystal Structure of the Ribonucleoprotein Core of the Signal Recognition ParticleScience, 2000
- RNAs that bind and change the permeability of phospholipid membranesProceedings of the National Academy of Sciences, 1999
- Structure of the phylogenetically most conserved domain of SRP RNARNA, 1999
- Structure of the most conserved internal loop in SRP RNA.Nature Structural & Molecular Biology, 1999
- Structure of ?-lytic protease complexed with its pro regionNature Structural & Molecular Biology, 1998
- Crystal Structure of the Signal Sequence Binding Subunit of the Signal Recognition ParticleCell, 1998
- Ordered water molecules as key allosteric mediators in a cooperative dimeric hemoglobinProceedings of the National Academy of Sciences, 1996
- Structural basis of the allosteric behaviour of phosphofructokinaseNature, 1990
- Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particleNature, 1989
- Human SRP RNA and E. coli 4.5S RNA contain a highly homologous structural domainCell, 1988