1f05: Difference between revisions
New page: left|200px<br /> <applet load="1f05" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f05, resolution 2.45Å" /> '''CRYSTAL STRUCTURE O... |
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[[Image:1f05.gif|left|200px]]<br /> | [[Image:1f05.gif|left|200px]]<br /><applet load="1f05" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1f05, resolution 2.45Å" /> | caption="1f05, resolution 2.45Å" /> | ||
'''CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE'''<br /> | '''CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of human transaldolase has been determined to 2.45 A | 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. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1F05 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Transaldolase Transaldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.2 2.2.1.2] Full crystallographic information is available from [http:// | 1F05 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Transaldolase Transaldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.2 2.2.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F05 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: alpha-beta barrel]] | [[Category: alpha-beta barrel]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:22 2008'' | ||
Revision as of 13:33, 21 February 2008
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CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Leukemia-1, T-cell acute lymphocytic OMIM:[187040], Transaldolase deficiency OMIM:[602063]
About this StructureAbout this Structure
1F05 is a Single protein structure of sequence from Homo sapiens. Active as Transaldolase, with EC number 2.2.1.2 Full crystallographic information is available from OCA.
ReferenceReference
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
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