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1t0w
From Proteopedia
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| - | [[Image:1t0w.gif|left|200px]] | + | [[Image:1t0w.gif|left|200px]] |
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| - | '''25 NMR structures of Truncated Hevein of 32 aa (Hevein-32) complex with N,N,N-triacetylglucosamina''' | + | {{Structure |
| + | |PDB= 1t0w |SIZE=350|CAPTION= <scene name='initialview01'>1t0w</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''25 NMR structures of Truncated Hevein of 32 aa (Hevein-32) complex with N,N,N-triacetylglucosamina''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1T0W is a [ | + | 1T0W is a [[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=1T0W OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15368576 15368576] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Aboitiz, N.]] | [[Category: Aboitiz, N.]] | ||
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[[Category: anti-parallel beta-sheet]] | [[Category: anti-parallel beta-sheet]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:12:12 2008'' |
Revision as of 12:12, 20 March 2008
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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]. 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 Mar 20 14:12:12 2008
