Related ArticlesNMR 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 of 1.00 A (backbone of the beta-domain) from 1075 experimental restraints obtained from multinuclear, multidimensional NMR experiments. The domain is observed to bind to its own C-terminus and offers a preview of the interaction of this chaperone with other proteins. The bound protein region is tightly held at a single amino acid position (a leucyl residue) that is buried in a deep pocket lined with conserved hydrophobic residues. A second hydrophobic binding site was identified using paramagnetically labeled peptides. It is located in a region close to the N-terminus of the domain and may constitute the allosteric region that links substrate-binding affinity with nucleotide binding in the Hsp70 chaperones.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
J Inorg Biochem. 2010 Oct;104(10):1063-70
Authors: Du Z, Unno M, Matsui T, Ikeda-Saito M, La Mar GN
Proton 2D NMR was used to confirm in solution a highly conserved portion of the molecular structure upon substrate loss for the...
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[NMR paper] Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Related Articles Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Biochemistry. 2004 Nov 2;43(43):13775-86
Authors: Bann JG, Frieden C
The folding of the two-domain bacterial chaperone PapD has been studied to develop an understanding of the relationship between individual domain folding and the formation of domain-domain interactions. PapD contains six phenylalanine residues, four in the N-terminal domain and two in the...
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[NMR paper] NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein
NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein that is selectively cytotoxic to cancer cells.
Related Articles NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein that is selectively cytotoxic to cancer cells.
Biochemistry. 2004 Feb 24;43(7):1854-61
Authors: Rosal R, Pincus MR, Brandt-Rauf PW, Fine RL, Michl J, Wang H
We have recently found that a peptide from the mdm-2 binding domain of the p53 protein induced rapid membranolytic necrosis of a variety of different human...
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[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...
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[NMR paper] NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin
NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin.
Related Articles NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin.
J Biol Chem. 2000 Jan 14;275(2):1089-94
Authors: Huang W, Dolmer K, Liao X, Gettins PG
Human alpha(2)-macroglobulin-proteinase complexes bind to their receptor, the low density lipoprotein receptor-related protein (LRP), through a discrete 138-residue C-terminal receptor binding domain (RBD), which also binds to the beta-amyloid peptide. We have used NMR...
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11-18-2010 09:15 PM
[NMR paper] NMR solution structure of the periplasmic chaperone FimC.
NMR solution structure of the periplasmic chaperone FimC.
Related Articles NMR solution structure of the periplasmic chaperone FimC.
Nat Struct Biol. 1998 Oct;5(10):885-90
Authors: Pellecchia M, Güntert P, Glockshuber R, Wüthrich K
The NMR structure of the 205-residue periplasmic chaperone FimC is presented. This protein consists of two globular domains with immunoglobulin-like folds connected by a 15-residue linker peptide. The relative orientation of the two domains is defined by hydrophobic contacts and an interdomain salt bridge. FimC...
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[NMR paper] NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reve
NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5.
EMBO J. 1995 Jul 17;14(14):3563-71
Authors: Bycroft M, Grünert S, Murzin AG, Proctor M, St Johnston D
The...
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[NMR paper] Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spec
Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy.
EMBO J. 1994 Sep 1;13(17):3936-44
Authors: Fogh RH, Ottleben G, Rüterjans H, Schnarr M, Boelens R, Kaptein R
The structure of the 84 residue DNA binding domain of the Escherichia coli LexA repressor has been determined from...