Crystal Structure of the Conserved Subdomain of Human Protein SRP54M at 2.1Å Resolution: Evidence for the Mechanism of Signal Peptide Binding
- 1 September 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 292 (3) , 697-705
- https://doi.org/10.1006/jmbi.1999.3090
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Expression, purification, and crystallography of the conserved methionine-rich domain of human signal recognition particle 54 kda proteinProtein Science, 1999
- Conformational variability of the N-terminal helix in the structure of ribosomal protein S15Structure, 1998
- Protein SRP54 of human signal recognition particle: cloning, expression, and comparative analysis of functional sitesGene, 1998
- Binding site of the M-domain of human protein SRP54 determined by systematic site-directed mutagenesis of signal recognition particle RNANucleic Acids Research, 1997
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992
- Determination of Macromolecular Structures from Anomalous Diffraction of Synchrotron RadiationScience, 1991
- Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particleNature, 1989
- Signal sequencesBiochemistry, 1989
- Crystallographic refinement by simulated annealingJournal of Molecular Biology, 1988
- Translocation in yeast and mammalian cells: not all signal sequences are functionally equivalent.The Journal of cell biology, 1987