1j8c
From Proteopedia
(New page: 200px<br /> <applet load="1j8c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j8c" /> '''Solution Structure of the Ubiquitin-like Do...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1j8c.gif|left|200px]]<br /> | + | [[Image:1j8c.gif|left|200px]]<br /><applet load="1j8c" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1j8c" size=" | + | |
caption="1j8c" /> | caption="1j8c" /> | ||
'''Solution Structure of the Ubiquitin-like Domain of hPLIC-2'''<br /> | '''Solution Structure of the Ubiquitin-like Domain of hPLIC-2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 26S proteasome is essential for the proteolysis of proteins that have | + | The 26S proteasome is essential for the proteolysis of proteins that have been covalently modified by the attachment of polyubiquitinated chains. Although the 20S core particle performs the degradation, the 19S regulatory cap complex is responsible for recognition of polyubiquitinated substrates. We have focused on how the S5a component of the 19S complex interacts with different ubiquitin-like (ubl) modules, to advance our understanding of how polyubiquitinated proteins are targeted to the proteasome. To achieve this, we have determined the solution structure of the ubl domain of hPLIC-2 and obtained a structural model of hHR23a by using NMR spectroscopy and homology modeling. We have also compared the S5a binding properties of ubiquitin, SUMO-1, and the ubl domains of hPLIC-2 and hHR23a and have identified the residues on their respective S5a contact surfaces. We provide evidence that the S5a-binding surface on the ubl domain of hPLIC-2 is required for its interaction with the proteasome. This study provides structural insights into protein recognition by the proteasome, and illustrates how the protein surface of a commonly utilized fold has highly evolved for various biological roles. |
==About this Structure== | ==About this Structure== | ||
| - | 1J8C 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:// | + | 1J8C 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=1J8C OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 13: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Goh, A | + | [[Category: Goh, A M.]] |
| - | [[Category: Howley, P | + | [[Category: Howley, P M.]] |
| - | [[Category: Kleijnen, M | + | [[Category: Kleijnen, M F.]] |
[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
| - | [[Category: Walters, K | + | [[Category: Walters, K J.]] |
[[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 13:19:48 2008'' |
Revision as of 11:19, 21 February 2008
|
Solution Structure of the Ubiquitin-like Domain of hPLIC-2
Overview
The 26S proteasome is essential for the proteolysis of proteins that have been covalently modified by the attachment of polyubiquitinated chains. Although the 20S core particle performs the degradation, the 19S regulatory cap complex is responsible for recognition of polyubiquitinated substrates. We have focused on how the S5a component of the 19S complex interacts with different ubiquitin-like (ubl) modules, to advance our understanding of how polyubiquitinated proteins are targeted to the proteasome. To achieve this, we have determined the solution structure of the ubl domain of hPLIC-2 and obtained a structural model of hHR23a by using NMR spectroscopy and homology modeling. We have also compared the S5a binding properties of ubiquitin, SUMO-1, and the ubl domains of hPLIC-2 and hHR23a and have identified the residues on their respective S5a contact surfaces. We provide evidence that the S5a-binding surface on the ubl domain of hPLIC-2 is required for its interaction with the proteasome. This study provides structural insights into protein recognition by the proteasome, and illustrates how the protein surface of a commonly utilized fold has highly evolved for various biological roles.
About this Structure
1J8C is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a., Walters KJ, Kleijnen MF, Goh AM, Wagner G, Howley PM, Biochemistry. 2002 Feb 12;41(6):1767-77. PMID:11827521
Page seeded by OCA on Thu Feb 21 13:19:48 2008
