1p98: Difference between revisions

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[[Image:1p98.gif|left|200px]]<br />

[[Image:1p98.gif|left|200px]]<br /><applet load="1p98" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1p98" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1p98" />

'''High-resolution NMR structure of the Ubl-domain of HHR23A'''<br />

==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==

1P98 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=1P98 OCA].

1P98 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=1P98 OCA].

==Reference==

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[[Category: Single protein]]

[[Category: Feigon, J.]]

[[Category: Mueller, T.D.]]

[[Category: Mueller, T D.]]

[[Category: ubiquitin-like domain]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 18~~:41:~~14 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:35 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1p98.gif|left|200px]]<br />
+[[Image:1p98.gif|left|200px]]<br /><applet load="1p98" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1p98" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1p98" />
 '''High-resolution NMR structure of the Ubl-domain of HHR23A'''<br />
 ==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==
-P98 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=1P98 OCA].
+P98 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=1P98 OCA].
 ==Reference==
@@ Line 15: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Feigon, J.]]
-[[Category: Mueller, T.D.]]
+[[Category: Mueller, T D.]]
 [[Category: ubiquitin-like domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:41:14 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:35 2008''