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''' | '''25 NMR structures of Truncated Hevein of 32 aa (Hevein-32) complex with N,N,N-triacetylglucosamina''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1T0W is a [[Single protein]] structure | + | 1T0W is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0W OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Jimenez-Barbero, J.]] | [[Category: Jimenez-Barbero, J.]] | ||
[[Category: Vila-Perello, M.]] | [[Category: Vila-Perello, M.]] | ||
| - | [[Category: | + | [[Category: Alpha-helix]] |
| - | [[Category: | + | [[Category: Anti-parallel beta-sheet]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:22:06 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:22, 3 May 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. 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 Sat May 3 09:22:06 2008
