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1p9c
From Proteopedia
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[[Image:1p9c.gif|left|200px]] | [[Image:1p9c.gif|left|200px]] | ||
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'''NMR solution structure of the C-terminal ubiquitin-interacting motif of the proteasome subunit S5a''' | '''NMR solution structure of the C-terminal ubiquitin-interacting motif of the proteasome subunit S5a''' | ||
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[[Category: Feigon, J.]] | [[Category: Feigon, J.]] | ||
[[Category: Mueller, T D.]] | [[Category: Mueller, T D.]] | ||
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| - | [[Category: | + | [[Category: Hairpin loop]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:50:46 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:50, 3 May 2008
NMR solution structure of the C-terminal ubiquitin-interacting motif of the proteasome subunit S5a
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.
About this Structure
1P9C is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 04:50:46 2008
