1p9d
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High-resolution structure of the complex of HHR23A ubiquitin-like domain and the C-terminal ubiquitin-interacting motif of 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
1P9D is a Protein complex structure of sequences 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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