title: Click synthesis of ubiquitin dimer analogs to interrogate linkage-specific UBA domain binding.
abstract: A new route to the synthesis of triazole-linked ubiquitin dimers (diUbs) as structural analogs of the seven diUbs is reported. Binding studies with the Lys48-specific UBA domain of the Mud1 protein suggest that they represent functionally suitable surrogates of their native counterparts linked by an isopeptide bond.
authors.affiliation: Institute of Biochemistry, University of Muenster, Wilhelm-Klemm-Str. 2, D-48149 Münster, Germany.
authors.forename: Nadine D
authors.initials: ND
authors.lastname: Weikart
authors.forename: Stefanie
authors.initials: S
authors.lastname: Sommer
authors.forename: Henning D
authors.initials: HD
authors.lastname: Mootz
mesh_terms: D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism; D057930:Click Chemistry / Q000379:methods*; D008958:Models, Molecular; D011485:Protein Binding; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D012568:Schizosaccharomyces / Q000737:chemistry / Q000378:metabolism; D029702:Schizosaccharomyces pombe Proteins / Q000737:chemistry / Q000378:metabolism; D025801:Ubiquitin / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*
chemical_list: D002352:Carrier Proteins; C504973:Mud1 protein, S pombe; D029702:Schizosaccharomyces pombe Proteins; D025801:Ubiquitin