NMR spectroscopy of 14-3-3? reveals a flexible C-terminal extension. Differentiation of the chaperone and phosphoserine binding activities of 14-3-3?
Biochem J. 2011 May 10;
Authors: Williams DM, Ecroyd H, Goodwin KL, Dai H, Fu H, Woodcock JM, Zhang L, Carver JA
Intracellular 14-3-3 proteins bind to many proteins, via a specific phosphoserine motif, regulating diverse cellular tasks including cell signalling and disease progression. The 14-3-3? isoform is a molecular chaperone, preventing the stress-induced aggregation of target proteins in a comparable manner to the unrelated small heat-shock proteins (sHsps). 1H NMR spectroscopy revealed the presence of a flexible and unstructured C-terminal extension, 12 amino acids in length, which protrudes from the domain core of 14-3-3? and is similar in structure and length to the C-terminal extension of mammalian sHsps. The extension stabilises 14-3-3? but has no direct role in chaperone action. K49 is an important functional residue within 14-3-3?'s ligand binding groove with K49E 14-3-3? exhibiting markedly reduced binding to phosphorylated and non-phosphorylated ligands. The R18 peptide binds to 14-3-3?'s binding groove with high affinity and also reduces 14-3-3?'s interactions with ligands. However, neither K49E 14-3-3? nor the presence of the R18 peptide affect 14-3-3?'s chaperone activity, implying that the C-terminal extension and binding groove of 14-3-3? do not mediate interaction with target proteins during chaperone action. Other region(s) in 14-3-3? are most likely involved, i.e. the protein's chaperone and phosphoserine binding activities are functionally and structurally separated.
PMID: 21554249 [PubMed - as supplied by publisher]
Probing the Interaction of Cisplatin with the Human Copper Chaperone Atox1 by Solution and In-Cell NMR Spectroscopy
Probing the Interaction of Cisplatin with the Human Copper Chaperone Atox1 by Solution and In-Cell NMR Spectroscopy
Fabio Arnesano, Lucia Banci, Ivano Bertini, Isabella C. Felli, Maurizio Losacco and Giovanni Natile
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja207346p/aop/images/medium/ja-2011-07346p_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja207346p
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/9nWkAzWuq20
nmrlearner
Journal club
0
10-24-2011 11:06 PM
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
J Biol Chem. 2011 May 3;
Authors: Shin J, Chakraborty G, Bharatham N, Kang C, Tochio N, Koshiba S, Kigawa T, Kim W, Kim KT, Yoon HS
Vaccinia-related kinase 1 (VRK1) is one of the mitotic kinases which play important roles in cell cycle, nuclear condensation and transcription regulation. Kinase...
nmrlearner
Journal club
0
05-06-2011 12:02 PM
NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin.
NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin.
Related Articles NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin.
Biochemistry. 2010 Dec 1;
Authors: Lange A, Hoeller D, Wienk H, Marcillat O, Lancelin JM, Walker O
The VHS domain of the Stam2 protein is a ubiquitin binding domain involved in the recognition of ubiquitinated proteins committed to lysosomal degradation. Among all VHS domains, the VHS domain of Stam proteins is the strongest binder to...
nmrlearner
Journal club
0
12-03-2010 08:52 PM
[NMR paper] Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with w
Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments.
Related Articles Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments.
Biochemistry. 2003 Sep 30;42(38):11100-8
Authors: Cai S, Stevens SY, Budor AP, Zuiderweg ER
The interaction of solvent of the substrate binding domain of the bacterial heat shock 70 chaperone protein DnaK was studied in its apo form and with bound hydrophobic substrate peptide, using refined nuclear magnetic...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Docking multiple conformations of a flexible ligand into a protein binding site using
Docking multiple conformations of a flexible ligand into a protein binding site using NMR restraints.
Related Articles Docking multiple conformations of a flexible ligand into a protein binding site using NMR restraints.
Proteins. 2002 Feb 15;46(3):295-307
Authors: Zabell AP, Post CB
A method is described for docking a large, flexible ligand using intra-ligand conformational restraints from exchange-transferred NOE (etNOE) data. Numerous conformations of the ligand are generated in isolation, and a subset of representative conformations is...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[NMR paper] NMR structure of the N-terminal domain of Saccharomyces cerevisiae RNase HI reveals a
NMR structure of the N-terminal domain of Saccharomyces cerevisiae RNase HI reveals a fold with a strong resemblance to the N-terminal domain of ribosomal protein L9.
Related Articles NMR structure of the N-terminal domain of Saccharomyces cerevisiae RNase HI reveals a fold with a strong resemblance to the N-terminal domain of ribosomal protein L9.
J Mol Biol. 1999 Aug 20;291(3):661-9
Authors: Evans SP, Bycroft M
In addition to the conserved and well-defined RNase H domain, eukaryotic RNases HI possess either one or two copies of a small...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[NMR paper] NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain:
NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.
Related Articles NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.
Biochemistry. 1998 Jun 2;37(22):7929-40
Authors: Wang H, Kurochkin AV, Pang Y, Hu W, Flynn GC, Zuiderweg ER
The solution structure of the 21 kDa substrate-binding domain of the Escherichia coli Hsp70-chaperone protein DnaK (DnaK 386-561) has been determined to a precision...
nmrlearner
Journal club
0
11-17-2010 11:06 PM
[NMR paper] 1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 1
1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids.
FEBS Lett. 1995 Aug 7;369(2-3):305-10
Authors: Carver JA, Esposito G, Schwedersky G, Gaestel M
The small heat-shock proteins (Hsps) exist as large aggregates and function by interacting and stabilising non-native proteins in...