Publications

BibTex format

@article{Krysztofinska:2017:10.3389/fmolb.2017.00068,
author = {Krysztofinska, EM and Evans, NJ and Thapaliya, A and Murray, JW and Morgan, RML and Martinez-Lumbreras, S and Isaacson, RL},
doi = {10.3389/fmolb.2017.00068},
journal = {Frontiers in Molecular Biosciences},
title = {Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp.},
url = {http://dx.doi.org/10.3389/fmolb.2017.00068},
volume = {4},
year = {2017}
}

Download

RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Small glutamine-rich tetratricopeptide repeat-containing protein 2 (Sgt2) is a multi-module co-chaperone involved in several protein quality control pathways. The TPR domain of Sgt2 and several other proteins, including SGTA, Hop, and CHIP, is a highly conserved motif known to form transient complexes with molecular chaperones such as Hsp70 and Hsp90. In this work, we present the first high resolution crystal structures of Sgt2_TPR alone and in complex with a C-terminal peptide PTVEEVD from heat shock protein, Ssa1. Using nuclear magnetic resonance spectroscopy and isothermal titration calorimetry, we demonstrate that Sgt2_TPR interacts with peptides corresponding to the C-termini of Ssa1, Hsc82, and Ybr137wp with similar binding modes and affinities.
AU  - Krysztofinska,EM
AU  - Evans,NJ
AU  - Thapaliya,A
AU  - Murray,JW
AU  - Morgan,RML
AU  - Martinez-Lumbreras,S
AU  - Isaacson,RL
DO  - 10.3389/fmolb.2017.00068
PY  - 2017///
SN  - 2296-889X
TI  - Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp.
T2  - Frontiers in Molecular Biosciences
UR  - http://dx.doi.org/10.3389/fmolb.2017.00068
UR  - http://hdl.handle.net/10044/1/53316
VL  - 4
ER  -

Download

DrJamesMurray

Contact

Location

Summary

Citation

BibTex format

RIS format (EndNote, RefMan)