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PDBsum entry 1j8c
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Structural genomics
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PDB id
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1j8c
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structural studies of the interaction between ubiquitin family proteins and proteasome subunit s5a.
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Authors
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K.J.Walters,
M.F.Kleijnen,
A.M.Goh,
G.Wagner,
P.M.Howley.
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Ref.
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Biochemistry, 2002,
41,
1767-1777.
[DOI no: ]
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PubMed id
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Abstract
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The 26S proteasome is essential for the proteolysis of proteins that have been
covalently modified by the attachment of polyubiquitinated chains. Although the
20S core particle performs the degradation, the 19S regulatory cap complex is
responsible for recognition of polyubiquitinated substrates. We have focused on
how the S5a component of the 19S complex interacts with different ubiquitin-like
(ubl) modules, to advance our understanding of how polyubiquitinated proteins
are targeted to the proteasome. To achieve this, we have determined the solution
structure of the ubl domain of hPLIC-2 and obtained a structural model of hHR23a
by using NMR spectroscopy and homology modeling. We have also compared the S5a
binding properties of ubiquitin, SUMO-1, and the ubl domains of hPLIC-2 and
hHR23a and have identified the residues on their respective S5a contact
surfaces. We provide evidence that the S5a-binding surface on the ubl domain of
hPLIC-2 is required for its interaction with the proteasome. This study provides
structural insights into protein recognition by the proteasome, and illustrates
how the protein surface of a commonly utilized fold has highly evolved for
various biological roles.
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