 |
PDBsum entry 1p9c
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Ligand binding protein
|
PDB id
|
|
|
|
1p9c
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural determinants for the binding of ubiquitin-Like domains to the proteasome.
|
|
|
Authors
|
|
T.D.Mueller,
J.Feigon.
|
|
|
Ref.
|
|
Embo J, 2003,
22,
4634-4645.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
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.
|
|
|
|
|
|
|
