6vin
From Proteopedia
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(New page: '''Unreleased structure''' The entry 6vin is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystallographic structure of the circularly permuted human Taspase1 protein== | |
| + | <StructureSection load='6vin' size='340' side='right'caption='[[6vin]], [[Resolution|resolution]] 3.04Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6vin]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VIN FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.04Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vin OCA], [https://pdbe.org/6vin PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vin RCSB], [https://www.ebi.ac.uk/pdbsum/6vin PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vin ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TASP1_HUMAN TASP1_HUMAN] Protease involved in MLL processing and, consequently, in the correct expression of the early HOXA gene cluster. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Taspase1 is an Ntn-hydrolase overexpressed in primary human cancers, coordinating cancer cell proliferation, invasion, and metastasis. Loss of Taspase1 activity disrupts proliferation of human cancer cells in vitro and in mouse models of glioblastoma. Taspase1 is synthesized as an inactive proenzyme, becoming active upon intramolecular cleavage. The activation process changes the conformation of a long fragment at the C-terminus of the alpha subunit, for which no full-length structural information exists and whose function is poorly understood. We present a cloning strategy to generate a circularly permuted form of Taspase1 to determine the crystallographic structure of active Taspase1. We discovered that this region forms a long helix and is indispensable for the catalytic activity of Taspase1. Our study highlights the importance of this element for the enzymatic activity of Ntn-hydrolases, suggesting that it could be a potential target for the design of inhibitors with potential to be developed into anticancer therapeutics. | ||
| - | + | Structural insights into the function of the catalytically active human Taspase1.,Nagaratnam N, Delker SL, Jernigan R, Edwards TE, Snider J, Thifault D, Williams D, Nannenga BL, Stofega M, Sambucetti L, Hsieh JJ, Flint AJ, Fromme P, Martin-Garcia JM Structure. 2021 Mar 25. pii: S0969-2126(21)00081-2. doi:, 10.1016/j.str.2021.03.008. PMID:33784495<ref>PMID:33784495</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6vin" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Fromme P]] | ||
| + | [[Category: Martin-Garcia JM]] | ||
Current revision
Crystallographic structure of the circularly permuted human Taspase1 protein
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