1ttn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(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...)
Line 1: Line 1:
-
[[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="450" color="white" frame="true" align="right" spinBox="true"
+
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, (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.
+
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==
==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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TTN OCA].
+
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==
Line 14: Line 13:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Hu, H.Y.]]
+
[[Category: Hu, H Y.]]
[[Category: dc-ubp]]
[[Category: dc-ubp]]
[[Category: nmr]]
[[Category: nmr]]
Line 20: Line 19:
[[Category: ubiquitin-like domain]]
[[Category: ubiquitin-like domain]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:27:58 2007''
+
''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


1ttn

Drag the structure with the mouse to rotate

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools