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2a8i

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Revision as of 16:36, 10 September 2015

Crystal Structure of human Taspase1

Structural highlights

2a8i is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[TASP1_HUMAN] Protease involved in MLL processing and, consequently, in the correct expression of the early HOXA gene cluster.

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 PubMed

Taspase1 catalyzes the proteolytic processing of the mixed lineage leukemia (MLL) nuclear protein, which is required for maintaining Hox gene expression patterns. Chromosomal translocations of the MLL gene are associated with leukemia in infants. Taspase1, a threonine aspartase, is a member of the type 2 asparaginase family, but is the only protease in this family. We report here the crystal structures of human activated Taspase1 and its proenzyme, as well as the characterization of the effects of mutations in the active site region using a newly developed fluorogenic assay. The structure of Taspase1 has significant differences from other asparaginases, especially near the active site. Mutation of the catalytic nucleophile, Thr234, abolishes autocatalytic processing in cis but does not completely block proteolysis in trans. The structure unexpectedly showed the binding of a chloride ion in the active site, and our kinetic studies confirm that chlorides ions are inhibitors of this enzyme at physiologically relevant concentrations.

Crystal structure of human Taspase1, a crucial protease regulating the function of MLL.,Khan JA, Dunn BM, Tong L Structure. 2005 Oct;13(10):1443-52. PMID:16216576^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Khan JA, Dunn BM, Tong L. Crystal structure of human Taspase1, a crucial protease regulating the function of MLL. Structure. 2005 Oct;13(10):1443-52. PMID:16216576 doi:10.1016/j.str.2005.07.006

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2a8i"

@@ Line 4: / Line 4: @@
 <table><tr><td colspan='2'>[[2a8i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A8I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A8I FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=2a8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a8i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2a8i RCSB], [http://www.ebi.ac.uk/pdbsum/2a8i 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=2a8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a8i OCA], [http://pdbe.org/2a8i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a8i RCSB], [http://www.ebi.ac.uk/pdbsum/2a8i PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2a8i" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2a8i

From Proteopedia

Revision as of 16:36, 10 September 2015

Crystal Structure of human Taspase1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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