1f05

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{{STRUCTURE_1f05| PDB=1f05 | SCENE= }}
{{STRUCTURE_1f05| PDB=1f05 | SCENE= }}
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'''CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE'''
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===CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 10869557 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10869557}}
==About this Structure==
==About this Structure==
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[[Category: Thorell, S.]]
[[Category: Thorell, S.]]
[[Category: Alpha-beta barrel]]
[[Category: Alpha-beta barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:44:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:17:08 2008''

Revision as of 23:17, 30 June 2008

Image:1f05.png

Template:STRUCTURE 1f05

CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE

Template:ABSTRACT PUBMED 10869557

About this Structure

1F05 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Tue Jul 1 02:17:08 2008

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