PDBsum entry: 1t0w

Sugar binding protein

PDB id: 1t0w

Contents

Protein chain

33 a.a. *

Ligands

NAG-NAG-NAG

* Residue conservation analysis

PDB id:

1t0w

Name:

Sugar binding protein

Title:

25 nmr structures of truncated hevein of 32 aa (hevein-32) c with n,n,n-triacetylglucosamina

Structure:

Hevein. Chain: a. Fragment: n-terminal domain. Synonym: allergen hev b 6. Engineered: yes

Source:

Synthetic: yes. Other_details: sequence prepared on a mbha resin by standar phase peptide synthesis protocols. The sequence of the pept naturally found in hevea brasiliensis (para rubber tree).

NMR struc:

25 models

Authors:

N.Aboitiz,M.Vila-Perello,P.Groves,J.L.Asensio,D.Andreu,F.J.C J.Jimenez-Barbero

Key ref:

N.Aboitiz et al. (2004). 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. Chembiochem, 5, 1245-1255. PubMed id: 15368576 DOI: 10.1002/cbic.200400025

Date:

13-Apr-04 Release date: 28-Sep-04

Protein chain

P02877  (HEVE_HEVBR) -  Pro-hevein

Seq: 204 a.a.

Struc: 33 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 

• Biochemical function: chitin binding (1 term)

DOI no: 10.1002/cbic.200400025

Chembiochem 5:1245-1255 (2004)

PubMed id: 15368576

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.

N.Aboitiz, M.Vila-Perelló, P.Groves, J.L.Asensio, D.Andreu, F.J.Cañada, J.Jiménez-Barbero.

ABSTRACT

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.