Related ArticlesNMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of a GNRA fold by an arginine-rich motif.
Cell. 1998 Apr 17;93(2):289-99
Authors: Legault P, Li J, Mogridge J, Kay LE, Greenblatt J
The structure of the complex formed by the arginine-rich motif of the transcriptional antitermination protein N of phage lambda and boxB RNA was determined by heteronuclear magnetic resonance spectroscopy. A bent alpha helix in N recognizes primarily the shape and negatively charged surface of the boxB hairpin through multiple hydrophobic and ionic interactions. The GAAGA boxB loop forms a GNRA fold, previously described for tetraloops, which is essential for N binding. The fourth nucleotide of the loop extrudes from the GNRA fold to enable the E. coli elongation factor NusA to recognize the N protein/RNA complex. This structure reveals a new mode of RNA-protein recognition and shows how a small RNA element can facilitate a protein-protein interaction and thereby nucleate formation of a large ribonucleoprotein complex.
[NMR paper] NMR assignment of the gpU tail protein from lambda bacteriophage.
NMR assignment of the gpU tail protein from lambda bacteriophage.
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J Biomol NMR. 2005 May;32(1):91-2
Authors: Edmonds L, Thirumoorthy R, Liu A, Davidson A, Donaldson L
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[NMR paper] NMR solution structure of the monomeric form of the bacteriophage lambda capsid stabi
NMR solution structure of the monomeric form of the bacteriophage lambda capsid stabilizing protein gpD.
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J Biomol NMR. 2005 Apr;31(4):351-6
Authors: Iwai H, Forrer P, Plückthun A, Güntert P
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[NMR paper] NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface i
NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface important for co-receptor binding.
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Structure. 2000 Apr 15;8(4):385-95
Authors: Tugarinov V, Zvi A, Levy R, Hayek Y, Matsushita S, Anglister J
BACKGROUND: The protein 0.5beta is a potent strain-specific human immunodeficiency virus type 1 (HIV-1) neutralizing antibody raised against the entire envelope glycoprotein (gp120) of...
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[NMR paper] NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+
NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump.
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Biochemistry. 1999 Sep 21;38(38):12320-32
Authors: Elshorst B, Hennig M, Försterling H, Diener A, Maurer M, Schulte P, Schwalbe H, Griesinger C, Krebs J, Schmid H, Vorherr T, Carafoli E
The three-dimensional structure of the complex between calmodulin (CaM) and a peptide corresponding to the N-terminal portion of the CaM-binding domain of the...
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[NMR paper] Recognition of DNA by GAL4 in solution: use of a monomeric protein-DNA complex for st
Recognition of DNA by GAL4 in solution: use of a monomeric protein-DNA complex for study by NMR.
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Biochemistry. 1994 Mar 15;33(10):3071-8
Authors: Baleja JD, Mau T, Wagner G
The complex of a monomer of GAL4 with DNA has been investigated by two-dimensional 1H nuclear magnetic resonance (NMR) spectroscopy. Previous X-ray analysis has revealed a structure in which a dimer of the N-terminal 65-residue fragment of GAL4 forms a complex,...
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[NMR paper] Recognition of DNA by GAL4 in solution: use of a monomeric protein-DNA complex for st
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Biochemistry. 1994 Mar 15;33(10):3071-8
Authors: Baleja JD, Mau T, Wagner G
The complex of a monomer of GAL4 with DNA has been investigated by two-dimensional 1H nuclear magnetic resonance (NMR) spectroscopy. Previous X-ray analysis has revealed a structure in which a dimer of the N-terminal 65-residue fragment of GAL4 forms a complex,...
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[NMR paper] 1H NMR studies of DNA recognition by the glucocorticoid receptor: complex of the DNA
1H NMR studies of DNA recognition by the glucocorticoid receptor: complex of the DNA binding domain with a half-site response element.
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Biochemistry. 1991 Dec 17;30(50):11620-4
Authors: Remerowski ML, Kellenbach E, Boelens R, van der Marel GA, van Boom JH, Maler BA, Yamamoto KR, Kaptein R
The complex of the rat glucocorticoid receptor (GR) DNA binding domain (DBD) and half-site sequence of the...
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[NMR paper] 1H NMR studies of DNA recognition by the glucocorticoid receptor: complex of the DNA
1H NMR studies of DNA recognition by the glucocorticoid receptor: complex of the DNA binding domain with a half-site response element.
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Biochemistry. 1991 Dec 17;30(50):11620-4
Authors: Remerowski ML, Kellenbach E, Boelens R, van der Marel GA, van Boom JH, Maler BA, Yamamoto KR, Kaptein R
The complex of the rat glucocorticoid receptor (GR) DNA binding domain (DBD) and half-site sequence of the...
NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of
Linear Mode
