2AN6

Protein-peptide complex

Summary for 2AN6

• Entry DOI: 10.2210/pdb2an6/pdb
• Descriptor: Ubiquitin ligase SIAH1A, peptide from Phyllopod, ZINC ION (3 entities in total)
• Functional Keywords: protein-peptide complex, ligase
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cytoplasm: P61092
• Total number of polymer chains: 8
• Total formula weight: 98071.50

Authors

House, C.M.,Hancock, N.C.,Moller, A.,Cromer, B.A.,Fedorov, V.,Bowtell, D.D.L.,Parker, M.W.,Polekhina, G. (deposition date: 2005-08-11, release date: 2006-05-30, Last modification date: 2024-03-13)

Primary citation

House, C.M.,Hancock, N.C.,Moller, A.,Cromer, B.A.,Fedorov, V.,Bowtell, D.D.L.,Parker, M.W.,Polekhina, G.
Elucidation of the substrate binding site of Siah ubiquitin ligase
Structure, 14:695-701, 2006

PubMed 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.

PubMed: 16615911
DOI: 10.1016/j.str.2005.12.013

Experimental method

X-RAY DIFFRACTION (3 Å)