Related ArticlesNMR study on the major mite allergen Der f 2: its refined tertiary structure, epitopes for monoclonal antibodies and characteristics shared by ML protein group members.
J Biochem. 2005 Mar;137(3):255-63
Authors: Ichikawa S, Takai T, Inoue T, Yuuki T, Okumura Y, Ogura K, Inagaki F, Hatanaka H
Group 2 major mite allergens Der f 2 and Der p 2 are classified into the recently identified group of MD-2-related lipid-recognition (ML) proteins, but the ligands and biological functions of these allergens are unknown. We have obtained a high-quality NMR structure for Der f 2, and found that it is more similar to the crystal structure of NPC2, a distant homologue, than to that of Der p 2, in terms of the separation and angle between the two major beta-sheets. This made us propose that ML proteins undergo clamshell-like motions that change the sizes of ligand-binding spaces inside their immunoglobulin-fold beta-sandwich to accommodate lipid molecules. This type of motion in lipopolysaccaride recognition of MD-2 is suggested to be likely as well by structural models. We also report the applicability of NMR differential exchange broadening experiments for complexes of intact monoclonal antibodies and antigens; using this technique, we have detected the conformational epitopes for monoclonal antibodies 15E11 and 13A4 as two separate surface patches.
[NMR paper] Refined NMR structure of alpha-sarcin by 15N-1H residual dipolar couplings.
Refined NMR structure of alpha-sarcin by 15N-1H residual dipolar couplings.
Related Articles Refined NMR structure of alpha-sarcin by 15N-1H residual dipolar couplings.
Eur Biophys J. 2005 Nov;34(8):1057-65
Authors: García-Mayoral MF, Pantoja-Uceda D, Santoro J, Martínez del Pozo A, Gavilanes JG, Rico M, Bruix M
(15)N-(1)H residual dipolar couplings (RDC) have been used as additional restraints to refine the solution structure of the ribotoxin alpha-sarcin. The RDC values were obtained by partial alignment of alpha-sarcin in the binary mixture...
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[NMR paper] NMR solution structure of Ole e 6, a major allergen from olive tree pollen.
NMR solution structure of Ole e 6, a major allergen from olive tree pollen.
Related Articles NMR solution structure of Ole e 6, a major allergen from olive tree pollen.
J Biol Chem. 2004 Sep 10;279(37):39035-41
Authors: Treviño MA, García-Mayoral MF, Barral P, Villalba M, Santoro J, Rico M, Rodríguez R, Bruix M
Ole e 6 is a pollen protein from the olive tree (Olea europaea) that exhibits allergenic activity with a high prevalence among olive-allergic individuals. The three-dimensional structure of Ole e 6 has been determined in solution by NMR...
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[NMR paper] Refined solution structure and backbone dynamics of 15N-labeled C12A-p8MTCP1 studied
Refined solution structure and backbone dynamics of 15N-labeled C12A-p8MTCP1 studied by NMR relaxation.
Related Articles Refined solution structure and backbone dynamics of 15N-labeled C12A-p8MTCP1 studied by NMR relaxation.
J Biomol NMR. 1999 Dec;15(4):271-88
Authors: Barthe P, Chiche L, Declerck N, Delsuc MA, Lefèvre JF, Malliavin T, Mispelter J, Stern MH, Lhoste JM, Roumestand C
MTCP1 (for Mature-T-Cell Proliferation) was the first gene unequivocally identified in the group of uncommon leukemias with a mature phenotype. The...
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[NMR paper] NMR study suggests a major role for Arg111 in maintaining the structure and dynamical
NMR study suggests a major role for Arg111 in maintaining the structure and dynamical properties of type II human cellular retinoic acid binding protein.
Related Articles NMR study suggests a major role for Arg111 in maintaining the structure and dynamical properties of type II human cellular retinoic acid binding protein.
Biochemistry. 1998 Sep 15;37(37):13021-32
Authors: Wang L, Yan H
The solution structure of a site-directed mutant of type-II human cellular retinoic acid binding protein (CRABPII) with Arg111 replaced by methionine (R111M)...
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[NMR paper] Reexamination of the secondary and tertiary structure of histidine-containing protein
Reexamination of the secondary and tertiary structure of histidine-containing protein from Escherichia coli by homonuclear and heteronuclear NMR spectroscopy.
Related Articles Reexamination of the secondary and tertiary structure of histidine-containing protein from Escherichia coli by homonuclear and heteronuclear NMR spectroscopy.
Biochemistry. 1991 Dec 24;30(51):11842-50
Authors: Hammen PK, Waygood EB, Klevit RE
Analysis of the histidine-containing protein (HPr) from Escherichia coli by two-dimensional homonuclear and heteronuclear nuclear...
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[NMR paper] Reexamination of the secondary and tertiary structure of histidine-containing protein
Reexamination of the secondary and tertiary structure of histidine-containing protein from Escherichia coli by homonuclear and heteronuclear NMR spectroscopy.
Related Articles Reexamination of the secondary and tertiary structure of histidine-containing protein from Escherichia coli by homonuclear and heteronuclear NMR spectroscopy.
Biochemistry. 1991 Dec 24;30(51):11842-50
Authors: Hammen PK, Waygood EB, Klevit RE
Analysis of the histidine-containing protein (HPr) from Escherichia coli by two-dimensional homonuclear and heteronuclear nuclear...
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[NMR paper] Tertiary structure of two-electron reduced Megasphaera elsdenii flavodoxin and some i
Tertiary structure of two-electron reduced Megasphaera elsdenii flavodoxin and some implications, as determined by two-dimensional 1H-NMR and restrained molecular dynamics.
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 Tertiary structure of two-electron reduced Megasphaera elsdenii flavodoxin and some implications, as determined by two-dimensional 1H-NMR and restrained molecular dynamics.
Eur J Biochem. 1990 Nov 26;194(1):185-98
Authors: ...
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[NMR paper] Secondary and tertiary structure characteristics of Megasphaera elsdenii flavodoxin i
Secondary and tertiary structure characteristics of Megasphaera elsdenii flavodoxin in the reduced state as determined by two-dimensional 1H NMR.
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 Secondary and tertiary structure characteristics of Megasphaera elsdenii flavodoxin in the reduced state as determined by two-dimensional 1H NMR.
Eur J Biochem. 1990 May 20;189(3):589-600
Authors: van Mierlo CP, Müller F, Vervoort J
The...