Related ArticlesComposition and sequence specific resonance assignments of the heterogeneous N-linked glycan in the 13.6 kDa adhesion domain of human CD2 as determined by NMR on the intact glycoprotein.
Biochemistry. 1995 Feb 7;34(5):1622-34
Authors: Wyss DF, Choi JS, Wagner G
CD2, a T cell specific surface adhesion receptor, is critically important for T lymphocytes to mediate their regulatory and effector functions. The amino terminal domain of human CD2 is responsible for cell adhesion, binding to CD58 on antigen-presenting cells or target cells. This adhesion domain in human CD2 contains a single high-mannose N-glycan. This carbohydrate or part of it appears to be required to maintain the native conformation of the polypeptide and its ability to bind CD58. To better understand the structural aspects that regulate human CD2 adhesion functions, we had previously determined the solution structure of the protein part of the N-glycosylated adhesion domain of human CD2 (hu-sCD2(105); MW approximately 13.6 kDa) by NMR spectroscopy. Here, we have identified protein--carbohydrate and carbohydrate--carbohydrate interactions and, in combination with previous knowledge from electrospray ionization mass spectrometry, have determined the composition of the heterogeneous high-mannose glycan in hu-sCD2(105). These contacts clearly define the carbohydrate's orientation with respect to the protein. The NMR data further suggest that one arm of the glycan is folded toward the trisaccharide core consisting of GlcNAc1-GlcNAc2-Man3. A detailed comparison between chemical shift data of free model oligosaccharides with those of the glycomers present in our hu-sCD2(105) sample reveals that only the resonances of the two GlcNAc residues are significantly different from those of free high-mannose glycans. This work was based on a new strategy to achieve sequential assignments of the 1H and 13C resonances of the heterogeneous high-mannose carbohydrate [(Man)nGlcNAc2, n = 5-8] in hu-sCD2(105) on the intact glycoprotein using a combination of homonuclear 1H-1H and heteronuclear 1H-13C NMR experiments at natural abundance.
[NMR paper] Sequence-specific NMR resonance assignments of the backbone atoms for the olfactory m
Sequence-specific NMR resonance assignments of the backbone atoms for the olfactory marker protein, OMP.
Related Articles Sequence-specific NMR resonance assignments of the backbone atoms for the olfactory marker protein, OMP.
J Biomol NMR. 2000 Aug;17(4):353-4
Authors: Baldisseri DM, Margolis JW, Omotosho PA, Volkman BF, Margolis FL
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[NMR paper] Sequence-specific 1H NMR resonance assignments and secondary structure of human apoli
Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate.
Related Articles Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate.
Biochem Cell Biol. 1998;76(2-3):267-75
Authors: Rozek A, Sparrow JT, Weisgraber KH, Cushley RJ
Apolipoprotein (apo) C-I is a 57-residue exchangeable plasma protein distributed mainly in high and very low density lipoprotein. In this report we...
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[NMR paper] Sequence-specific resonance assignments of the 1H-NMR spectra and structural characte
Sequence-specific resonance assignments of the 1H-NMR spectra and structural characterization in solution of the HIV-1 transframe protein p6.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Sequence-specific resonance assignments of the 1H-NMR spectra and structural characterization in solution of the HIV-1 transframe protein p6.
Eur J Biochem. 1996 Apr 15;237(2):383-92
Authors: Beissinger M, Paulus C, Bayer P, Wolf H, Rösch P, Wagner R
...
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[NMR paper] Sequence-specific resonance assignments of the 1H-NMR spectra of a synthetic, biologi
Sequence-specific resonance assignments of the 1H-NMR spectra of a synthetic, biologically active EIAV Tat protein.
Related Articles Sequence-specific resonance assignments of the 1H-NMR spectra of a synthetic, biologically active EIAV Tat protein.
Biochemistry. 1993 Aug 24;32(33):8439-45
Authors: Willbold D, Krüger U, Frank R, Rosin-Arbesfeld R, Gazit A, Yaniv A, Rösch P
The equine infectious anemia virus (EIAV) trans-activating (Tat) protein is a close homologue of the human immunodeficiency virus (HIV) Tat protein. Both of these proteins...
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[NMR paper] A constraint reasoning system for automating sequence-specific resonance assignments
A constraint reasoning system for automating sequence-specific resonance assignments from multidimensional protein NMR spectra.
Related Articles A constraint reasoning system for automating sequence-specific resonance assignments from multidimensional protein NMR spectra.
Proc Int Conf Intell Syst Mol Biol. 1993;1:447-55
Authors: Zimmerman DE, Kulikowski CA, Montelione GT
AUTOASSIGN is a prototype expert system designed to aid in the determination of protein structure from nuclear magnetic resonance (NMR) measurements. In this paper we focus...
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[NMR paper] Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spect
Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spectra obtained from mutants to resolve spectral overlap.
Related Articles Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spectra obtained from mutants to resolve spectral overlap.
Biochemistry. 1990 Aug 7;29(31):7191-200
Authors: Wittekind M, Reizer J, Klevit RE
On the basis of an analysis of two-dimensional 1H NMR spectra, the complete sequence-specific 1H NMR assignments are presented for the phosphocarrier protein HPr from the...
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[NMR paper] An efficient NMR approach for obtaining sequence-specific resonance assignments of la
An efficient NMR approach for obtaining sequence-specific resonance assignments of larger proteins based on multiple isotopic labeling.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles An efficient NMR approach for obtaining sequence-specific resonance assignments of larger proteins based on multiple isotopic labeling.
FEBS Lett. 1990 Jun 18;266(1-2):155-8
Authors: Ikura M, Krinks M, Torchia DA, Bax A
By simultaneously incorporating in a protein 13C-carbonyl- and...
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[NMR paper] Sequence-specific [1H]NMR resonance assignments and secondary structure identificatio
Sequence-specific NMR resonance assignments and secondary structure identification for 1- and 2-zinc finger constructs from SW15. A hydrophobic core involving four invariant residues.
Related Articles Sequence-specific NMR resonance assignments and secondary structure identification for 1- and 2-zinc finger constructs from SW15. A hydrophobic core involving four invariant residues.
FEBS Lett. 1990 Mar 26;262(2):179-84
Authors: Neuhaus D, Nakaseko Y, Nagai K, Klug A
Complete NMR resonance assignments are presented for the second of the three...