The Crystal Structure of a Self-Activating G Protein α Subunit Reveals Its Distinct Mechanism of Signal Initiation
Janice C. Jones, Jeffrey W. Duffy, Mischa Machius, Brenda R. S. Temple, Henrik G. Dohlman,* Alan M. Jones
*To whom correspondence should be addressed. E-mail:
This PDF file includes:
- Fig. S1. Solvent accessibility of guanine nucleotides in plant and animal G protein α subunits.
- Fig. S2. B value analysis of AtGPA1.
- Fig. S3. Nucleotide exchange by G protein α subunits.
- Fig. S4. CD spectra of GDP-bound G protein α subunits.
- Table S1. Data collection and refinement statistics for AtGPA1.
- Table S2. GTP-binding rates for wild-type and mutant G protein α subunits.
- Movie S1 legend.
Format: Adobe Acrobat PDF
Size: 391 KB
Other Supplementary Material for this manuscript includes the following:
- Table S3 (Microsoft Excel format). B value analysis of crystal structures of G protein α subunits. 67 KB
- Movie S1 (.avi format). Movie depicting domain motion in AtGPA1 generated from MD simulations. 8.6 MB
Citation: J. C. Jones, J. W. Duffy, M. Machius, B. R. S. Temple, H. G. Dohlman, A. M. Jones, The Crystal Structure of a Self-Activating G Protein α Subunit Reveals Its Distinct Mechanism of Signal Initiation. Sci. Signal. 4, ra8 (2011).