Elucidation of the Substrate Binding Site of Siah Ubiquitin Ligase Export

@article{citeulike:582350, abstract = {SummaryThe 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.}, author = {House, Colin M. and Hancock, Nancy C. and Moller, Andreas and Cromer, Brett A. and Fedorov, Victor and Bowtell, David D. and Parker, Michael W. and Polekhina, Galina}, citeulike-article-id = {582350}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.str.2005.12.013}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6VSR-4JP9G5W-D/2/6b7271ca04ba6281e10632359d5d5f1c}, doi = {10.1016/j.str.2005.12.013}, journal = {Structure}, keywords = {structure, ubiquitin}, month = {April}, number = {4}, pages = {695--701}, posted-at = {2006-04-11 21:25:32}, priority = {5}, title = {Elucidation of the Substrate Binding Site of Siah Ubiquitin Ligase}, url = {http://dx.doi.org/10.1016/j.str.2005.12.013}, volume = {14}, year = {2006} }

TY - JOUR ID - citeulike:582350 L3 - citeulike-article-id:582350 N2 - SummaryThe 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. IS - 4 JF - Structure EP - 701 TI - Elucidation of the Substrate Binding Site of Siah Ubiquitin Ligase VL - 14 SP - 695 KW - structure KW - ubiquitin AU - House, Colin AU - Hancock, Nancy AU - Moller, Andreas AU - Cromer, Brett AU - Fedorov, Victor AU - Bowtell, David AU - Parker, Michael AU - Polekhina, Galina PY - 2006/04// UR - http://dx.doi.org/10.1016/j.str.2005.12.013 ER -