1p9c: Difference between revisions

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New page: left|200px<br /> <applet load="1p9c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p9c" /> '''NMR solution structure of the C-terminal ub...
 
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[[Image:1p9c.gif|left|200px]]<br />
[[Image:1p9c.gif|left|200px]]<br /><applet load="1p9c" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1p9c" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1p9c" />
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'''NMR solution structure of the C-terminal ubiquitin-interacting motif of the proteasome subunit S5a'''<br />
'''NMR solution structure of the C-terminal ubiquitin-interacting motif of the proteasome subunit S5a'''<br />


==Overview==
==Overview==
HHR23A, a protein implicated in nucleotide excision repair, belongs to a, class of proteins containing both a ubiquitin-like (Ubl) domain and one or, more ubiquitin-associated (UBA) domains, suggesting a role in the, ubiquitin-proteasome pathway as well. The Ubl domain binds with high, affinity to the second ubiquitin-interacting motif (UIM) of the S5a, subunit of the proteasome. Here we present the solution structures of the, HHR23A Ubl domain, the second UIM of S5a (UIM-2), and the Ubl:S5a-UIM-2, complex. The HHR23A Ubl domain is structurally similar to ubiquitin. The, S5a UIM forms an alpha-helix with an unexpected hairpin loop that, contributes to the binding interface with Ubl. The molecular determinants, of the Ubl-proteasome interaction are revealed by analysis of the, structures, chemical shift mapping, mutant binding studies and sequence, conservation.
HHR23A, a protein implicated in nucleotide excision repair, belongs to a class of proteins containing both a ubiquitin-like (Ubl) domain and one or more ubiquitin-associated (UBA) domains, suggesting a role in the ubiquitin-proteasome pathway as well. The Ubl domain binds with high affinity to the second ubiquitin-interacting motif (UIM) of the S5a subunit of the proteasome. Here we present the solution structures of the HHR23A Ubl domain, the second UIM of S5a (UIM-2), and the Ubl:S5a-UIM-2 complex. The HHR23A Ubl domain is structurally similar to ubiquitin. The S5a UIM forms an alpha-helix with an unexpected hairpin loop that contributes to the binding interface with Ubl. The molecular determinants of the Ubl-proteasome interaction are revealed by analysis of the structures, chemical shift mapping, mutant binding studies and sequence conservation.


==About this Structure==
==About this Structure==
1P9C 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=1P9C OCA].  
1P9C 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=1P9C OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Feigon, J.]]
[[Category: Feigon, J.]]
[[Category: Mueller, T.D.]]
[[Category: Mueller, T D.]]
[[Category: alpha helix]]
[[Category: alpha helix]]
[[Category: hairpin loop]]
[[Category: hairpin loop]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:30 2008''

Revision as of 15:26, 21 February 2008

File:1p9c.gif


1p9c

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NMR solution structure of the C-terminal ubiquitin-interacting motif of the proteasome subunit S5a

OverviewOverview

HHR23A, a protein implicated in nucleotide excision repair, belongs to a class of proteins containing both a ubiquitin-like (Ubl) domain and one or more ubiquitin-associated (UBA) domains, suggesting a role in the ubiquitin-proteasome pathway as well. The Ubl domain binds with high affinity to the second ubiquitin-interacting motif (UIM) of the S5a subunit of the proteasome. Here we present the solution structures of the HHR23A Ubl domain, the second UIM of S5a (UIM-2), and the Ubl:S5a-UIM-2 complex. The HHR23A Ubl domain is structurally similar to ubiquitin. The S5a UIM forms an alpha-helix with an unexpected hairpin loop that contributes to the binding interface with Ubl. The molecular determinants of the Ubl-proteasome interaction are revealed by analysis of the structures, chemical shift mapping, mutant binding studies and sequence conservation.

About this StructureAbout this Structure

1P9C is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural determinants for the binding of ubiquitin-like domains to the proteasome., Mueller TD, Feigon J, EMBO J. 2003 Sep 15;22(18):4634-45. PMID:12970176

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