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New page: left|200px<br /> <applet load="1ttn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ttn" /> '''Solution structure of the ubiquitin-like do...
 
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[[Image:1ttn.gif|left|200px]]<br />
<applet load="1ttn" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Solution structure of the ubiquitin-like domain of human DC-UBP from dendritic cells'''<br />


==Overview==
==Solution structure of the ubiquitin-like domain of human DC-UBP from dendritic cells==
The previously identified dendritic cell-derived ubiquitin-like protein, (DC-UbP) was implicated in cellular differentiation and apoptosis., Sequence alignment suggested that it contains a ubiquitin-like (UbL), domain in the C terminus. Here, we present the solution NMR structure and, backbone dynamics of the UbL domain of DC-UbP. The overall structure of, the domain is very similar to that of Ub despite low similarity (&lt;30%) in, amino-acid sequence. One distinct feature of the domain structure is its, highly positively charged surface that is different from the corresponding, surfaces of the well-known UbL modifiers, Ub, NEDD8, and SUMO-1. The key, amino-acid residues responsible for guiding polyubiquitinated proteins to, proteasome degradation in Ub are not conserved in the UbL domain. This, implies that the UbL domain of DC-UbP may have its own specific, interaction partners with other yet unknown cellular functions related to, the Ub pathway.
<StructureSection load='1ttn' size='340' side='right'caption='[[1ttn]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ttn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TTN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1ttn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ttn OCA], [https://pdbe.org/1ttn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ttn RCSB], [https://www.ebi.ac.uk/pdbsum/1ttn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ttn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UBTD2_HUMAN UBTD2_HUMAN]
== 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/tt/1ttn_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1ttn ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The previously identified dendritic cell-derived ubiquitin-like protein (DC-UbP) was implicated in cellular differentiation and apoptosis. Sequence alignment suggested that it contains a ubiquitin-like (UbL) domain in the C terminus. Here, we present the solution NMR structure and backbone dynamics of the UbL domain of DC-UbP. The overall structure of the domain is very similar to that of Ub despite low similarity (&lt;30%) in amino-acid sequence. One distinct feature of the domain structure is its highly positively charged surface that is different from the corresponding surfaces of the well-known UbL modifiers, Ub, NEDD8, and SUMO-1. The key amino-acid residues responsible for guiding polyubiquitinated proteins to proteasome degradation in Ub are not conserved in the UbL domain. This implies that the UbL domain of DC-UbP may have its own specific interaction partners with other yet unknown cellular functions related to the Ub pathway.


==About this Structure==
Solution structure of the ubiquitin-like domain of human DC-UbP from dendritic cells.,Gao YG, Song AX, Shi YH, Chang YG, Liu SX, Yu YZ, Cao XT, Lin DH, Hu HY Protein Sci. 2005 Aug;14(8):2044-50. Epub 2005 Jun 29. PMID:15987890<ref>PMID:15987890</ref>
1TTN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TTN OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of the ubiquitin-like domain of human DC-UbP from dendritic cells., Gao YG, Song AX, Shi YH, Chang YG, Liu SX, Yu YZ, Cao XT, Lin DH, Hu HY, Protein Sci. 2005 Aug;14(8):2044-50. Epub 2005 Jun 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15987890 15987890]
</div>
<div class="pdbe-citations 1ttn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Hu, H.Y.]]
[[Category: Hu HY]]
[[Category: dc-ubp]]
[[Category: nmr]]
[[Category: solution structure]]
[[Category: ubiquitin-like domain]]
 
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Latest revision as of 18:16, 29 May 2024

Solution structure of the ubiquitin-like domain of human DC-UBP from dendritic cells

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