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PDBsum entry 3m63
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Ligase/protein binding
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PDB id
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3m63
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References listed in PDB file
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Key reference
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Title
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The yeast e4 ubiquitin ligase ufd2 interacts with the ubiquitin-Like domains of rad23 and dsk2 via a novel and distinct ubiquitin-Like binding domain.
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Authors
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P.Hänzelmann,
J.Stingele,
K.Hofmann,
H.Schindelin,
S.Raasi.
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Ref.
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J Biol Chem, 2010,
285,
20390-20398.
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PubMed id
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Abstract
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Proteins containing ubiquitin-like (UBL) and ubiquitin-associated (UBA) domains
interact with various binding partners and function as hubs during
ubiquitin-mediated protein degradation. A common interaction of the budding
yeast UBL-UBA proteins Rad23 and Dsk2 with the E4 ubiquitin ligase Ufd2 has been
described in endoplasmic reticulum-associated degradation among other pathways.
The UBL domains of Rad23 and Dsk2 play a prominent role in this process by
interacting with Ufd2 and different subunits of the 26 S proteasome. Here, we
report crystal structures of Ufd2 in complex with the UBL domains of Rad23 and
Dsk2. The N-terminal UBL-interacting region of Ufd2 exhibits a unique sequence
pattern, which is distinct from any known ubiquitin- or UBL-binding domain
identified so far. Residue-specific differences exist in the interactions of
these UBL domains with Ufd2, which are coupled to subtle differences in their
binding affinities. The molecular details of their differential interactions
point to a role for adaptive evolution in shaping these interfaces.
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