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The three-dimensional structure of human transaldolase
S Thorell1, P Gergely, K Banki
1Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
FEBS Letters
|June 28, 2000
Summary
The crystal structure of human transaldolase was determined, revealing an alpha/beta barrel fold common to class I aldolases. Key active site and hydrophobic core residues are conserved, with surface peptides potentially targeted in multiple sclerosis.
Area of Science:
- Biochemistry
- Structural Biology
- Immunology
Background:
- Human transaldolase is an enzyme implicated as an autoantigen in multiple sclerosis.
- Understanding its structure is crucial for elucidating its role in autoimmune responses.
Purpose of the Study:
- To determine the crystal structure of human transaldolase.
- To identify conserved residues and potential autoantigenic sites.
Main Methods:
- X-ray crystallography to determine the enzyme's 3D structure at 2.45 A resolution.
- Structure-based sequence alignment of the transaldolase subfamily.
Main Results:
- The enzyme exhibits an alpha/beta barrel fold, characteristic of class I aldolases.
- Eight invariant active site residues and a five-residue hydrophobic cluster were identified.
- Four immunodominant peptide segments on the enzyme's surface were located, accessible to autoantibodies.
Conclusions:
- The determined structure provides insights into transaldolase function and its similarity to other aldolases.
- Conserved residues highlight functionally important regions.
- Surface-exposed peptide segments may be targets for autoantibodies in multiple sclerosis.