Related ArticlesThe solution NMR structure of Antheraea polyphemus PBP provides new insight into pheromone recognition by pheromone-binding proteins.
J Mol Biol. 2004 Mar 19;337(2):443-51
Authors: Mohanty S, Zubkov S, Gronenborn AM
Pheromone-binding proteins (PBPs) located in the antennae of male moth species play an important role in olfaction. They are carrier proteins, believed to transport volatile hydrophobic pheromone molecules across the aqueous sensillar lymph to the membrane-bound G protein-coupled olfactory receptor proteins. The roles of PBPs in molecular recognition and the mechanisms of pheromone binding and release are poorly understood. Here, we report the NMR structure of a PBP from the giant silk moth Antheraea polyphemus. This is the first structure of a PBP with specific acetate-binding function in vivo. The protein consists of nine alpha-helices: alpha1a (residues 2-5), alpha1b (8-12), alpha1c (16-23), alpha2 (27-34), alpha3a (46-52), alpha3b (54-59), alpha4 (70-79), alpha5 (84-100) and alpha6 (107-125), held together by three disulfide bridges: 19-54, 50-108 and 97-117. A large hydrophobic cavity is located inside the protein, lined with side-chains from all nine helices. The acetate-binding site is located at the narrow end of the cavity formed by the helices alpha3b and alpha4. The pheromone can enter this cavity through an opening between the helix alpha1a, the C-terminal end of the helix alpha6, and the loop between alpha2 and alpha3a. We suggest that Trp37 may play an important role in the initial interaction with the ligand. Our analysis also shows that Asn53 plays the key role in recognition of acetate pheromones specifically, while Phe12, Phe36, Trp37, Phe76, and Phe118 are responsible for non-specific binding, and Leu8 and Ser9 may play a role in ligand chain length recognition.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Angew Chem Int Ed Engl. 2011 Sep 16;
Authors: Schanda P, Huber M, Boisbouvier J, Meier BH, Ernst M
PMID: 21928443
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09-20-2011 03:10 PM
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Angew Chem Int Ed Engl. 2011 Sep 14;
Authors: Schanda P, Huber M, Boisbouvier J, Meier BH, Ernst M
PMID: 21915969
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09-15-2011 08:31 PM
Insight into interactions of the von-Willebrand-factor-A-like domain 2 with the FNIII-like domain 9 of collagen VII by NMR and SPR.
Insight into interactions of the von-Willebrand-factor-A-like domain 2 with the FNIII-like domain 9 of collagen VII by NMR and SPR.
Insight into interactions of the von-Willebrand-factor-A-like domain 2 with the FNIII-like domain 9 of collagen VII by NMR and SPR.
FEBS Lett. 2011 May 9;
Authors: Leineweber S, Schönig S, Seeger K
Type VII collagen as component of anchoring fibrils plays an important role in skin architecture, however, no detailed structural information is available. Here, we describe the recombinant expression, isotope labeling, and...
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05-17-2011 06:21 PM
Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: Insight into intrinsically disordered proteins.
Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: Insight into intrinsically disordered proteins.
Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: Insight into intrinsically disordered proteins.
J Biol Chem. 2011 Apr 20;
Authors: Iwasa H, Meshitsuka S, Hongo K, Mizobata T, Kawata Y
Co-chaperonin GroES from E. coli works with chaperonin GroEL to mediate the folding reactions of various proteins. However, under specific conditions, i. e., the...
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04-22-2011 02:00 PM
[NMR paper] Molecular insight into the electrostatic membrane surface potential by 14n/31p MAS NM
Molecular insight into the electrostatic membrane surface potential by 14n/31p MAS NMR spectroscopy: nociceptin-lipid association.
Related Articles Molecular insight into the electrostatic membrane surface potential by 14n/31p MAS NMR spectroscopy: nociceptin-lipid association.
J Am Chem Soc. 2005 May 11;127(18):6610-6
Authors: Lindström F, Williamson PT, Gröbner G
Exploiting naturally abundant (14)N and (31)P nuclei by high-resolution MAS NMR (magic angle spinning nuclear magnetic resonance) provides a molecular view of the electrostatic...
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11-25-2010 08:21 PM
[NMR paper] Structural insight into human Zn(2+)-bound S100A2 from NMR and homology modeling.
Structural insight into human Zn(2+)-bound S100A2 from NMR and homology modeling.
Related Articles Structural insight into human Zn(2+)-bound S100A2 from NMR and homology modeling.
Biochem Biophys Res Commun. 2001 Oct 26;288(2):462-7
Authors: Randazzo A, Acklin C, Schäfer BW, Heizmann CW, Chazin WJ
The S100 subfamily of EF-hand proteins is distinguished by the binding of Zn(2+) in addition to Ca(2+). In an effort to understand the role of Zn(2+) in modulating the activity of S100 proteins, we have carried out heteronuclear NMR studies of...
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11-19-2010 08:44 PM
[NMR paper] Insight into the mechanism of serpin-proteinase inhibition from 2D [1H-15N] NMR studi
Insight into the mechanism of serpin-proteinase inhibition from 2D NMR studies of the 69 kDa alpha 1-proteinase inhibitor Pittsburgh-trypsin covalent complex.
Related Articles Insight into the mechanism of serpin-proteinase inhibition from 2D NMR studies of the 69 kDa alpha 1-proteinase inhibitor Pittsburgh-trypsin covalent complex.
Biochemistry. 2001 May 29;40(21):6284-92
Authors: Peterson FC, Gettins PG
We have used -HSQC NMR to investigate the structural changes that occur in both serpin and proteinase in forming the kinetically trapped...
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11-19-2010 08:32 PM
[NMR paper] NMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding pro
NMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding properties of this zinc binuclear cluster protein.
Related Articles NMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding properties of this zinc binuclear cluster protein.
J Mol Biol. 2000 Jan 28;295(4):729-36
Authors: Cerdan R, Cahuzac B, Félenbok B, Guittet E
The three-dimensional structure of the DNA-binding domain (residues 1-60) of the ethanol regulon transcription factor AlcR from Aspergillus nidulans has been solved by NMR....