1f05: Difference between revisions
No edit summary |
No edit summary |
||
| Line 2: | Line 2: | ||
<StructureSection load='1f05' size='340' side='right' caption='[[1f05]], [[Resolution|resolution]] 2.45Å' scene=''> | <StructureSection load='1f05' size='340' side='right' caption='[[1f05]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1f05]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1f05]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F05 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1onr|1onr]], [[1ucw|1ucw]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1onr|1onr]], [[1ucw|1ucw]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f05 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f05 RCSB], [http://www.ebi.ac.uk/pdbsum/1f05 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f05 OCA], [http://pdbe.org/1f05 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f05 RCSB], [http://www.ebi.ac.uk/pdbsum/1f05 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
| Line 29: | Line 29: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1f05" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
| Line 36: | Line 37: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Transaldolase]] | [[Category: Transaldolase]] | ||
[[Category: Schneider, G]] | [[Category: Schneider, G]] | ||
Revision as of 15:04, 10 September 2015
CRYSTAL STRUCTURE OF HUMAN TRANSALDOLASECRYSTAL STRUCTURE OF HUMAN TRANSALDOLASE
Structural highlights
Disease[TALDO_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. Function[TALDO_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 |
| ||||||||||||||||||