1zwu
From Proteopedia
(New page: 200px<br /><applet load="1zwu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zwu" /> '''30 NMR structures of AcAMP2-like peptide wit...) |
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| - | [[Image:1zwu.gif|left|200px]]<br /><applet load="1zwu" size=" | + | [[Image:1zwu.gif|left|200px]]<br /><applet load="1zwu" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''30 NMR structures of AcAMP2-like peptide with non natural beta-(2-naphthyl)-alanine residue.'''<br /> | '''30 NMR structures of AcAMP2-like peptide with non natural beta-(2-naphthyl)-alanine residue.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The specific interaction of a variety of modified hevein domains to | + | The specific interaction of a variety of modified hevein domains to chitooligosaccharides has been studied by NMR spectroscopy in order to assess the importance of aromatic-carbohydrate interactions for the molecular recognition of neutral sugars. These mutant AcAMP2-like peptides, which have 4-fluoro-phenylalanine, tryptophan, or 2-naphthylalanine at the key interacting positions, have been prepared by solid-phase synthesis. Their three-dimensional structures, when bound to the chitin-derived trisaccharide, have been deduced by NMR spectroscopy. By using DYANA and restrained molecular dynamics simulations with the AMBER 5.0 force field, the three-dimensional structures of the protein-sugar complexes have been obtained. The thermodynamic analysis of the interactions that occur upon complex formation have also been carried out. Regarding binding affinity, the obtained data have permitted the deduction that the larger the aromatic group, the higher the association constant and the binding enthalpy. In all cases, entropy opposes binding. In contrast, deactivation of the aromatic rings by attaching fluorine atoms decreases the binding affinity, with a concomitant decrease in enthalpy. The role of the chemical nature of the aromatic ring for establishing sugar contacts has been thus evaluated. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZWU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1ZWU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZWU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Andreu, C.]] | [[Category: Andreu, C.]] | ||
[[Category: Asensio, G.]] | [[Category: Asensio, G.]] | ||
| - | [[Category: Asensio, J | + | [[Category: Asensio, J L.]] |
| - | [[Category: Canada, F | + | [[Category: Canada, F J.]] |
| - | [[Category: Chavez, M | + | [[Category: Chavez, M I.]] |
[[Category: Freire, F.]] | [[Category: Freire, F.]] | ||
[[Category: Groves, P.]] | [[Category: Groves, P.]] | ||
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[[Category: anti-parallel beta-sheet.]] | [[Category: anti-parallel beta-sheet.]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:50 2008'' |
Revision as of 14:19, 21 February 2008
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30 NMR structures of AcAMP2-like peptide with non natural beta-(2-naphthyl)-alanine residue.
Overview
The specific interaction of a variety of modified hevein domains to chitooligosaccharides has been studied by NMR spectroscopy in order to assess the importance of aromatic-carbohydrate interactions for the molecular recognition of neutral sugars. These mutant AcAMP2-like peptides, which have 4-fluoro-phenylalanine, tryptophan, or 2-naphthylalanine at the key interacting positions, have been prepared by solid-phase synthesis. Their three-dimensional structures, when bound to the chitin-derived trisaccharide, have been deduced by NMR spectroscopy. By using DYANA and restrained molecular dynamics simulations with the AMBER 5.0 force field, the three-dimensional structures of the protein-sugar complexes have been obtained. The thermodynamic analysis of the interactions that occur upon complex formation have also been carried out. Regarding binding affinity, the obtained data have permitted the deduction that the larger the aromatic group, the higher the association constant and the binding enthalpy. In all cases, entropy opposes binding. In contrast, deactivation of the aromatic rings by attaching fluorine atoms decreases the binding affinity, with a concomitant decrease in enthalpy. The role of the chemical nature of the aromatic ring for establishing sugar contacts has been thus evaluated.
About this Structure
1ZWU is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
On the importance of carbohydrate-aromatic interactions for the molecular recognition of oligosaccharides by proteins: NMR studies of the structure and binding affinity of AcAMP2-like peptides with non-natural naphthyl and fluoroaromatic residues., Chavez MI, Andreu C, Vidal P, Aboitiz N, Freire F, Groves P, Asensio JL, Asensio G, Muraki M, Canada FJ, Jimenez-Barbero J, Chemistry. 2005 Nov 18;11(23):7060-74. PMID:16220560
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