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1ttn
From Proteopedia
(New page: 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 /> | + | [[Image:1ttn.gif|left|200px]]<br /><applet load="1ttn" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ttn" size=" | + | |
caption="1ttn" /> | caption="1ttn" /> | ||
'''Solution structure of the ubiquitin-like domain of human DC-UBP from dendritic cells'''<br /> | '''Solution structure of the ubiquitin-like domain of human DC-UBP from dendritic cells'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The previously identified dendritic cell-derived ubiquitin-like protein | + | 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 (<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== | ==About this Structure== | ||
| - | 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:// | + | 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1TTN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hu, H | + | [[Category: Hu, H Y.]] |
[[Category: dc-ubp]] | [[Category: dc-ubp]] | ||
[[Category: nmr]] | [[Category: nmr]] | ||
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[[Category: ubiquitin-like domain]] | [[Category: ubiquitin-like domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:12 2008'' |
Revision as of 13:17, 21 February 2008
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Solution structure of the ubiquitin-like domain of human DC-UBP from dendritic cells
Overview
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 (<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
1TTN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 15:17:12 2008
