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Title
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The three-dimensional structure of human transaldolase.
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Authors
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S.Thorell,
P.Gergely,
K.Banki,
A.Perl,
G.Schneider.
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Ref.
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FEBS Lett, 2000,
475,
205-208.
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PubMed id
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Abstract
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The crystal structure of human transaldolase has been determined to 2.45 A
resolution. The enzyme folds into an alpha/beta 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.
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