The three‐dimensional structure of human transaldolase

FEBS Letters

Thorell, Stina¹  Perl, Andras²  Schneider, Gunter¹  Gergely, Peter²  Banki, Katalin² 

[1] Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden;Department of Medicine and Microbiology and Immunology, College of Medicine, State University of New York, Syracuse, NY 13210, USA

关键词: Transaldolase;    Class I aldolase;    Protein crystallography;    Multiple sclerosis;   

DOI  :  10.1016/S0014-5793(00)01658-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The crystal structure of human transaldolase has been determined to 2.45 Å resolution. The enzyme folds into an α/β barrel structure and is thus similar in structure to other class I aldolases. Structure-based sequence alignment of available sequences of the transaldolase subfamily reveals that eight active site residues are invariant in the whole subfamily. Other invariant residues are mainly involved in the formation of the hydrophobic core of the enzyme. Noteworthy is a hydrophobic cluster consisting of five invariant residues. Human transaldolase has been implicated as an autoantigen in multiple sclerosis and four immunodominant peptide segments are located at the surface of the enzyme, accessible to autoantibodies.

【 授权许可】

Unknown