3u30
Crystal structure of a linear-specific Ubiquitin fab bound to linear ubiquitinCrystal structure of a linear-specific Ubiquitin fab bound to linear ubiquitin
Structural highlights
Publication Abstract from PubMedPolyubiquitination is an essential posttranslational modification that plays critical roles in cellular signaling. PolyUb (polyubiquitin) chains are formed by linking the carboxyl-terminus of one Ub (ubiquitin) subunit to either a lysine residue or the amino-terminus of an adjacent Ub. Linkage through the amino-terminus results in linear polyubiquitination that has recently been demonstrated to be a key step in nuclear factor kappaB activation; however, tools to study linear chains have been lacking. We therefore engineered a linear-linkage-specific antibody that is functional in Western blot, immunoprecipitation, and immunofluorescence applications. A crystal structure of the linear-linkage-specific antibody Fab fragment in complex with linear diubiquitin provides molecular insight into the nature of linear chain specificity. We use the antibody to demonstrate that linear polyUb is up-regulated upon tumor necrosis factor alpha stimulation of cells, consistent with a critical role in nuclear factor kappaB signaling. This antibody provides an essential tool for further investigation of the function of linear chains. Engineering and structural characterization of a linear polyubiquitin-specific antibody.,Matsumoto ML, Dong KC, Yu C, Phu L, Gao X, Hannoush RN, Hymowitz SG, Kirkpatrick DS, Dixit VM, Kelley RF J Mol Biol. 2012 May 4;418(3-4):134-44. doi: 10.1016/j.jmb.2011.12.053. Epub 2011, Dec 29. PMID:22227388[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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