1t0w
From Proteopedia
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|PDB= 1t0w |SIZE=350|CAPTION= <scene name='initialview01'>1t0w</scene> | |PDB= 1t0w |SIZE=350|CAPTION= <scene name='initialview01'>1t0w</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1hev|1HEV]], [[1q9b|1Q9B]], [[1mmc|1MMC]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0w OCA], [http://www.ebi.ac.uk/pdbsum/1t0w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t0w RCSB]</span> | ||
}} | }} | ||
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[[Category: Jimenez-Barbero, J.]] | [[Category: Jimenez-Barbero, J.]] | ||
[[Category: Vila-Perello, M.]] | [[Category: Vila-Perello, M.]] | ||
| - | [[Category: NH2]] | ||
[[Category: alpha-helix]] | [[Category: alpha-helix]] | ||
[[Category: anti-parallel beta-sheet]] | [[Category: anti-parallel beta-sheet]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:40 2008'' |
Revision as of 20:49, 30 March 2008
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| Ligands: | , | ||||||
| Related: | 1HEV, 1Q9B, 1MMC
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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