Related ArticlesNMR identification of the Tom20 binding segment in mitochondrial presequences.
J Mol Biol. 2001 Feb 16;306(2):137-43
Authors: Muto T, Obita T, Abe Y, Shodai T, Endo T, Kohda D
Many mitochondrial proteins are synthesized in the cytosol as precursors with N-terminal presequences, and are imported into mitochondria with the aid of translocator protein complexes containing presequence-binding proteins. Tom20, a receptor protein which functions in an early step of the mitochondrial protein import, recognizes presequences with divergent amino acid sequences. Here, we report the identification of the segments involved in binding to Tom20 in mitochondrial presequences. We monitored the chemical shift perturbation of the NMR signals of five different 15N-labeled presequence peptides by the addition of the cytosolic receptor domain of rat or yeast Tom20. The perturbed segments occupy different positions, either near the N terminus or at the C terminus, in the presequences. Spin label experiments revealed that this is not due to different orientations of the presequence peptides bound to Tom20. The results presented here will offer a starting point to perform detailed analyses of Tom20-binding elements by systematic amino acid replacements.
[NMR paper] Calbindin D28K interacts with Ran-binding protein M: identification of interacting do
Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy.
Related Articles Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy.
Biochem Biophys Res Commun. 2003 Apr 18;303(4):1186-92
Authors: Lutz W, Frank EM, Craig TA, Thompson R, Venters RA, Kojetin D, Cavanagh J, Kumar R
Calbindin D(28K) is an EF-hand containing protein that plays a vital role in neurological function. We now show that calcium-loaded calbindin D(28K) interacts...
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[NMR paper] In silico and NMR identification of inhibitors of the IGF-I and IGF-binding protein-5
In silico and NMR identification of inhibitors of the IGF-I and IGF-binding protein-5 interaction.
Related Articles In silico and NMR identification of inhibitors of the IGF-I and IGF-binding protein-5 interaction.
J Med Chem. 2002 Dec 19;45(26):5655-60
Authors: Kamionka M, Rehm T, Beisel HG, Lang K, Engh RA, Holak TA
Recently we have determined the crystal structure of the insulin-like growth factor-I (IGF-I) in complex with the N-terminal domain of the IGF-binding protein-5 (IGFBP-5). Here we report results of computer screening for...
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[NMR paper] Identification of the bile acid-binding site of the ileal lipid-binding protein by ph
Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure.
Related Articles Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure.
J Biol Chem. 2001 Mar 9;276(10):7291-301
Authors: Kramer W, Sauber K, Baringhaus KH, Kurz M, Stengelin S, Lange G, Corsiero D, Girbig F, König W, Weyland C
...
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[NMR paper] Identification of the DNA binding surface of H-NS protein from Escherichia coli by he
Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy.
Related Articles Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy.
FEBS Lett. 1999 Jul 16;455(1-2):63-9
Authors: Shindo H, Ohnuki A, Ginba H, Katoh E, Ueguchi C, Mizuno T, Yamazaki T
The DNA binding domain of H-NS protein was studied with various N-terminal deletion mutant proteins and identified by gel retardation assay and heteronuclear 2D- and 3D-NMR...
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11-18-2010 08:31 PM
[NMR paper] Identification by NMR of the binding surface for the histidine-containing phosphocarr
Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system.
Biochemistry. 1997 Apr 15;36(15):4393-8
Authors: Garrett DS, Seok YJ,...
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[NMR paper] Identification by NMR of the binding surface for the histidine-containing phosphocarr
Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system.
Biochemistry. 1997 Apr 15;36(15):4393-8
Authors: Garrett DS, Seok YJ,...
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[NMR paper] Identification of the single-stranded DNA binding surface of the transcriptional coac
Identification of the single-stranded DNA binding surface of the transcriptional coactivator PC4 by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Identification of the single-stranded DNA binding surface of the transcriptional coactivator PC4 by NMR.
J Biol Chem. 1999 Feb 5;274(6):3693-9
Authors: Werten S, Wechselberger R, Boelens R, van der Vliet PC, Kaptein R
The C-terminal domain of the eukaryotic transcriptional cofactor PC4...
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[NMR paper] Identification of the ribosome binding sites of translation initiation factor IF3 by
Identification of the ribosome binding sites of translation initiation factor IF3 by multidimensional heteronuclear NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Identification of the ribosome binding sites of translation initiation factor IF3 by multidimensional heteronuclear NMR spectroscopy.
RNA. 1999 Jan;5(1):82-92
Authors: Sette M, Spurio R, van Tilborg P, Gualerzi CO, Boelens R
Titrations of Escherichia coli translation initiation...