• Corpus ID: 99458624

Structural Characterization and Interactions of the CFTR Regulatory Region

@inproceedings{Baker2010StructuralCA,
  title={Structural Characterization and Interactions of the CFTR Regulatory Region},
  author={Jennifer M Baker},
  year={2010}
}
The intrinsically disordered nonphosphorylated and phosphorylated R region of CFTR and its interactions with NBD1 and SLC26A3 STAS have been characterized at residuespecific resolution, primarily using NMR. Limited chemical shift dispersion indicates that the R region is intrinsically disordered in solution and that no global folding event occurs upon phosphorylation. Chemical shifts of backbone nuclei and sidechain carbons were assigned. SSP values indicate that phosphorylation acts as a… 
Alanine and proline content modulate global sensitivity to discrete perturbations in disordered proteins
TLDR
The experiments showed that changes in local PPII structure cause changes in Rh that are variable and that depend on the intrinsic chain propensities of PRO and ALA residues, demonstrating a mechanism for coupling local and global structure changes.
Intrinsic α helix propensities compact hydrodynamic radii in intrinsically disordered proteins
TLDR
To investigate sequence‐modulation of IDP Rh, disordered ensembles generated by a hard sphere collision model modified with a structure‐based parameterization of the solution energetics were used to parse the contributions of net charge, main chain dihedral angle bias, and excluded volume on hydrodynamic size.
Hydrodynamic Radii of Intrinsically Disordered Proteins Determined from Experimental Polyproline II Propensities
TLDR
Results from this study indicate that the hydrodynamic dimensions of IDPs are evidence of considerable sequence-dependent backbone propensities for PP II structure that qualitatively, if not quantitatively, match conformational propensITIES measured in peptides.
Beta turn propensity and a model polymer scaling exponent identify disordered proteins that phase separate
TLDR
Structural-based simulations find that transient β-turn structures reduce the desolvation penalty of forming a protein-rich phase, which may explain the increased propensity for turns in IDPs that are utilized biologically for phase separation.
Parametrization of Backbone Flexibility in a Coarse-Grained Force Field for Proteins (COFFDROP) Derived from All-Atom Explicit-Solvent Molecular Dynamics Simulations of All Possible Two-Residue Peptides.
TLDR
The results indicate that the COFFDROP force field is likely to find use in modeling the conformational behavior of intrinsically disordered proteins and multidomain proteins connected by flexible linkers.
TESTING THE ABILITY OF STANDARD MOLECULAR DYNAMIC SOFTWARE FORCE FIELDS TO ACCURATELY MODEL THE STRUCTURAL FEATURES OF INTRINSICALLY DISORDERED PROTEINS
TLDR
This document summarizes current capabilities, research and operational priorities, and plans for further studies that were established at the 2015 USGS workshop on quantitative hazard assessments of earthquake-triggered landsliding and liquefaction.

References

SHOWING 1-10 OF 156 REFERENCES
Intermolecular interaction between R domains of cystic fibrosis transmembrane conductance regulator.
TLDR
The hypothesis that R-R interaction occurs and is stronger in the P3A-R mutants is tested, which corroborates the data from the channel study and supports the hypothesis that this mechanism plays a role in channel gating.
CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices
TLDR
Evidence for a dynamic complex with NBD1 that transiently engages different sites of the R region suggests a structural explanation for the dependence of CFTR activity on multiple PKA phosphorylation sites.
A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering.
TLDR
The demonstration that conformational behavior of unfolded proteins can be accurately predicted from the primary sequence by using a simple set of rules has important consequences for the understanding of the structure and dynamics of the unstructured state.
Expression and characterization of the NBD1-R domain region of CFTR: evidence for subunit-subunit interactions.
TLDR
Analysis of phosphorylation sites indicated that inhibition involved multiple sites in NBD1-R, including serines 660, 712, 737, 795, and 813, and suggests a novel mechanism for regulation of CFTRosphorylation.
Long-Range Interactions Within a Nonnative Protein
TLDR
NMR spectroscopy and site-directed mutagenesis data show that nativelike structure in the denatured protein is stabilized by the involvement of Trp62 in nonnative and long-range interactions.
Effect of phosphorylation on α-helix stability as a function of position
We have investigated the effect of placing phosphoserine at the N-cap, N1, N2, N3, and interior position in alanine-based α-helical peptides. Helix contents of each peptide were measured by CD
Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels.
Structural analysis of delta131delta, a fragment model of the denatured state of staphylococcal nuclease, has been extended by obtaining long-range distance restraints between protein chain segments
Highly populated turn conformations in natively unfolded tau protein identified from residual dipolar couplings and molecular simulation.
TLDR
Local sequence-dependent conformational tendencies interrupt the propensity to sample more extended conformations in adjacent strands and are remarkably resistant to local environmental factors, as demonstrated by the persistence of the RDC signature even under harsh denaturing conditions (8 M urea).
...
1
2
3
4
5
...