This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1t0w
From Proteopedia
(New page: 200px<br /><applet load="1t0w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t0w" /> '''25 NMR structures of Truncated Hevein of 32 ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1t0w.gif|left|200px]]<br /><applet load="1t0w" size=" | + | [[Image:1t0w.gif|left|200px]]<br /><applet load="1t0w" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t0w" /> | caption="1t0w" /> | ||
'''25 NMR structures of Truncated Hevein of 32 aa (Hevein-32) complex with N,N,N-triacetylglucosamina'''<br /> | '''25 NMR structures of Truncated Hevein of 32 aa (Hevein-32) complex with N,N,N-triacetylglucosamina'''<br /> | ||
==Overview== | ==Overview== | ||
| - | HEV32, a 32-residue, truncated hevein lacking eleven C-terminal amino | + | HEV32, a 32-residue, truncated hevein lacking eleven C-terminal amino acids, was synthesized by solid-phase methodology and correctly folded with three cysteine bridge pairs. The affinities of HEV32 for small chitin fragments--in the forms of N,N',N"-triacetylchitotriose ((GlcNAc)3) (millimolar) and N,N',N",N"',N"",N""'-hexaacetylchitohexaose ((GlcNAc)6) (micromolar)--as measured by NMR and fluorescence methods, are comparable with those of native hevein. The HEV32 ligand-binding process is enthalpy driven, while entropy opposes binding. The NMR structure of ligand-bound HEV32 in aqueous solution was determined to be highly similar to the NMR structure of ligand-bound hevein. Solvated molecular-dynamics simulations were performed in order to monitor the changes in side-chain conformation of the binding site of HEV32 and hevein upon interaction with ligands. The calculations suggest that the Trp21 side-chain orientation of HEV32 in the free form differs from that in the bound state; this agrees with fluorescence and thermodynamic data. HEV32 provides a simple molecular model for studying protein-carbohydrate interactions and for understanding the physiological relevance of small native hevein domains lacking C-terminal residues. |
==About this Structure== | ==About this Structure== | ||
| - | 1T0W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1T0W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0W OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Aboitiz, N.]] | [[Category: Aboitiz, N.]] | ||
[[Category: Andreu, D.]] | [[Category: Andreu, D.]] | ||
| - | [[Category: Asensio, J | + | [[Category: Asensio, J L.]] |
| - | [[Category: Canada, F | + | [[Category: Canada, F J.]] |
[[Category: Groves, P.]] | [[Category: Groves, P.]] | ||
[[Category: Jimenez-Barbero, J.]] | [[Category: Jimenez-Barbero, J.]] | ||
| Line 23: | Line 23: | ||
[[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 15:08:39 2008'' |
Revision as of 13:08, 21 February 2008
|
25 NMR structures of Truncated Hevein of 32 aa (Hevein-32) complex with N,N,N-triacetylglucosamina
Overview
HEV32, a 32-residue, truncated hevein lacking eleven C-terminal amino acids, was synthesized by solid-phase methodology and correctly folded with three cysteine bridge pairs. The affinities of HEV32 for small chitin fragments--in the forms of N,N',N"-triacetylchitotriose ((GlcNAc)3) (millimolar) and N,N',N",N"',N"",N""'-hexaacetylchitohexaose ((GlcNAc)6) (micromolar)--as measured by NMR and fluorescence methods, are comparable with those of native hevein. The HEV32 ligand-binding process is enthalpy driven, while entropy opposes binding. The NMR structure of ligand-bound HEV32 in aqueous solution was determined to be highly similar to the NMR structure of ligand-bound hevein. Solvated molecular-dynamics simulations were performed in order to monitor the changes in side-chain conformation of the binding site of HEV32 and hevein upon interaction with ligands. The calculations suggest that the Trp21 side-chain orientation of HEV32 in the free form differs from that in the bound state; this agrees with fluorescence and thermodynamic data. HEV32 provides a simple molecular model for studying protein-carbohydrate interactions and for understanding the physiological relevance of small native hevein domains lacking C-terminal residues.
About this Structure
1T0W is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.
Reference
NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides., Aboitiz N, Vila-Perello M, Groves P, Asensio JL, Andreu D, Canada FJ, Jimenez-Barbero J, Chembiochem. 2004 Sep 6;5(9):1245-55. PMID:15368576
Page seeded by OCA on Thu Feb 21 15:08:39 2008
