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Electron Transfer Partners of Cytochrome P450
The most recent advances being made in understanding the function of P450 redox partners and the electron transfer process are reviewed.
The Structure of the Talin Head Reveals a Novel Extended Conformation of the FERM Domain
RIAM and Vinculin Binding to Talin Are Mutually Exclusive and Regulate Adhesion Assembly and Turnover*
The structural characterization of the talin rod is reported, which proposes a model in which RIAM binding to R2R3 initially recruits talin to membranes where it activates integrins and recruits vinculin to stabilize the complex.
Mapping and Consensus Sequence Identification for Multiple Vinculin Binding Sites within the Talin Rod*
The interaction between the cytoskeletal proteins talin and vinculin plays a key role in integrin-mediated cell adhesion and migration and the specificity of this interaction is defined by spot-synthesizing a series of 25-mer talin VBS1 peptides containing substitutions with all the commonly occurring amino acids.
NMR of macromolecules : a practical approach
- G. Roberts
- Chemistry, Biology
Sample preparation Instrumentation and pulse sequences Resonance assignment strategies for small proteins Stable isotope labelling and resonance assignments in larger proteins Effects of chemical…
Crystal structure of the FMN‐binding domain of human cytochrome P450 reductase at 1.93 Å resolution
- Qiang Zhao, S. Modi, H. Driessen
- Biology, ChemistryProtein science : a publication of the Protein…
The crystal structure of P450R‐FMN reported here confirms the overall similarity of its α‐β‐α architecture to that of the bacterial flavodoxins, but reveals differences in the position, number, and length of the helices relative to the central β‐sheet.
The structure of the C-terminal actin-binding domain of talin
Electron microscopy provides direct evidence for binding of the dimer to F‐actin and indicates that it binds to three monomers along the long‐pitch helix of the actin filament.
Structure of a double ubiquitin-like domain in the talin head: a role in integrin activation
Solution structures of F0, F1 and of the F0F1 double domain are reported, suggesting that extensive interactions between the talin FERM domain and acidic membrane phospholipids are required to orientate the F ERM domain such that it can activate integrins.
Isolation and characterisation of two degradation products derived from the peptide antibiotic nisin
Domain Motion in Cytochrome P450 Reductase
- J. Ellis, A. Gutiérrez, I. Barsukov, Wei-Cheng Huang, J. Grossmann, G. Roberts
- PhysicsThe Journal of Biological Chemistry
- 26 October 2009
NMR and small-angle x-ray scattering experiments addressing the question of domain organization in human CPR showed that oxidized and NADPH-reduced CPRs have different overall shapes, suggesting that this conformational equilibrium is physiologically relevant.