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CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASECRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE
Structural highlights
DiseaseTALDO_HUMAN Defects in TALDO1 are the cause of transaldolase 1 deficiency (TALDO1 deficiency) [MIM:606003. It results in telangiectases of the skin, hepatosplenomegaly, and enlarged clitoris. FunctionTALDO_HUMAN Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. The three-dimensional structure of human transaldolase.,Thorell S, Gergely P Jr, Banki K, Perl A, Schneider G FEBS Lett. 2000 Jun 23;475(3):205-8. PMID:10869557[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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