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PMID:16615911

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Citation

House, CM, Hancock, NC, Möller, A, Cromer, BA, Fedorov, V, Bowtell, DD, Parker, MW and Polekhina, G (2006) Elucidation of the substrate binding site of Siah ubiquitin ligase. Structure 14:695-701

Abstract

The Siah family of RING proteins function as ubiquitin ligase components, contributing to the degradation of multiple targets involved in cell growth, differentiation, angiogenesis, oncogenesis, and inflammation. Previously, a binding motif (degron) was recognized in many of the Siah degradation targets, suggesting that Siah itself may facilitate substrate recognition. We report the crystal structure of the Siah in complex with a peptide containing the degron motif. Binding is within a groove formed in part by the zinc fingers and the first two beta strands of the TRAF-C domain of Siah. We show that residues in the degron, previously described to facilitate binding to Siah, interact with the protein. Mutagenesis of Siah at sites of interaction also abrogates both in vitro peptide binding and destabilization of a known Siah target.

Links

PubMed Online version:10.1016/j.str.2005.12.013

Keywords

Amino Acid Motifs; Animals; Binding Sites; Cell Differentiation; Cell Line; Cloning, Molecular; Crystallography, X-Ray; Early Growth Response Transcription Factors/chemistry; Glutathione Transferase/metabolism; Humans; Inflammation; Kruppel-Like Transcription Factors/chemistry; Mice; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Neovascularization, Pathologic; Nuclear Proteins/chemistry; Nuclear Proteins/metabolism; Peptides/chemistry; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Proteins/chemistry; Proteins/metabolism; Time Factors; Transfection; Ubiquitin-Protein Ligases/chemistry; Ubiquitin-Protein Ligases/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

MOUSE:SIA1A

involved_in

GO:0006511: ubiquitin-dependent protein catabolic process

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

MOUSE:SIA1A

enables

GO:0008270: zinc ion binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

MOUSE:SIA1A

enables

GO:0004842: ubiquitin-protein transferase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

MOUSE:SIA1A

enables

GO:0042803: protein homodimerization activity

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P61092

F

Seeded From UniProt

complete

MOUSE:SIA1A

involved_in

GO:0043161: proteasome-mediated ubiquitin-dependent protein catabolic process

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

MOUSE:SIA1A

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q27934

F

Seeded From UniProt

complete

DROME:PHYL

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P61092

F

Seeded From UniProt

complete


See also

References

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