1vec
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:1vec.png|left|200px]] | ||
- | < | + | ==Crystal structure of the N-terminal domain of rck/p54, a human DEAD-box protein== |
- | + | <StructureSection load='1vec' size='340' side='right'caption='[[1vec]], [[Resolution|resolution]] 2.01Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[1vec]] 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=1VEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VEC 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]] 2.01Å</td></tr> | |
- | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1vec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vec OCA], [https://pdbe.org/1vec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vec RCSB], [https://www.ebi.ac.uk/pdbsum/1vec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vec ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Disease == | ||
+ | [https://www.uniprot.org/uniprot/DDX6_HUMAN DDX6_HUMAN] Note=A chromosomal aberration involving DDX6 may be a cause of hematopoietic tumors such as B-cell lymphomas. Translocation t(11;14)(q23;q32). | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/DDX6_HUMAN DDX6_HUMAN] In the process of mRNA degradation, may play a role in mRNA decapping. | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ve/1vec_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1vec ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Human rck/p54, a product of the gene cloned at the breakpoint of t(11; 14) (q23;q32) chromosomal translocation on 11q23 in B-cell lymphoma, is a member of the DEAD-box RNA helicase family. Here, the crystal structure of Nc-rck/p54, the N-terminal core domain of rck/p54, revealed that the P-loop in motif I formed a closed conformation, which was induced by Asn131, a residue unique to the RCK subfamily. It appears that ATP does not bind to the P-loop. The results of dynamic light scattering revealed to ATP-induced conformational change of rck/p54. It was demonstrated that free rck/p54 is a distended molecule in solution, and that the approach between N-terminal core and C-terminal domains for ATP binding would be essential when unwinding RNA. The results from helicase assay using electron micrograph, ATP hydrolytic and luciferase assay showed that c-myc IRES RNA, whose secondary structure regulates IRES-dependant translation, was unwound by rck/p54 and indicated that it is a good substrate for rck/p54. Over-expression of rck/p54 in HeLa cells caused growth inhibition and cell cycle arrest at G2/M with down-regulation of c-myc expression. These findings altogether suggest that rck/p54 may affect the IRES-dependent translation of c-myc even in the cells. | ||
- | + | Structural insight of human DEAD-box protein rck/p54 into its substrate recognition with conformational changes.,Matsui T, Hogetsu K, Usukura J, Sato T, Kumasaka T, Akao Y, Tanaka N Genes Cells. 2006 Apr;11(4):439-52. PMID:16611246<ref>PMID:16611246</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 1vec" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Helicase 3D structures|Helicase 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | |
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- | == | + | |
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Hogetsu | + | [[Category: Hogetsu K]] |
- | [[Category: Kumasaka | + | [[Category: Kumasaka T]] |
- | [[Category: Matsui | + | [[Category: Matsui T]] |
- | [[Category: Sato | + | [[Category: Sato T]] |
- | [[Category: Tanaka | + | [[Category: Tanaka M]] |
- | [[Category: Tanaka | + | [[Category: Tanaka N]] |
- | [[Category: Yukihiro | + | [[Category: Yukihiro Y]] |
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Current revision
Crystal structure of the N-terminal domain of rck/p54, a human DEAD-box protein
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Categories: Homo sapiens | Large Structures | Hogetsu K | Kumasaka T | Matsui T | Sato T | Tanaka M | Tanaka N | Yukihiro Y