title: Protein heterodimerization through ligand-bridged multivalent pre-organization: enhancing ligand binding toward both protein targets.
abstract: Structure-based design of a bifunctional ligand for two protein pentamers, cholera toxin B pentamer (CTB) and human serum amyloid P component (SAP), leads to multivalent dimerization of CTB and SAP in solution. This multivalent heterodimerization of proteins significantly enhances the affinity of the bifunctional ligand toward both target proteins.
authors.affiliation: Biomolecular Structure Center, Department of Chemistry, University of Washington, Seattle, Washington 98195, USA.
authors.forename: Jiyun
authors.initials: J
authors.lastname: Liu
authors.forename: Zhongsheng
authors.initials: Z
authors.lastname: Zhang
authors.forename: Xiaojian
authors.initials: X
authors.lastname: Tan
authors.forename: Wim G J
authors.initials: WG
authors.lastname: Hol
authors.forename: Christophe L M J
authors.initials: CL
authors.lastname: Verlinde
authors.forename: Erkang
authors.initials: E
authors.lastname: Fan
mesh_terms: D002772:Cholera Toxin / Q000737:chemistry*; D019281:Dimerization; D007700:Kinetics; D008024:Ligands; D011392:Proline / Q000031:analogs & derivatives* / Q000737:chemistry; D011485:Protein Binding; D000683:Serum Amyloid P-Component / Q000737:chemistry*; D013329:Structure-Activity Relationship
chemical_list: D008024:Ligands; D000683:Serum Amyloid P-Component; D002772:Cholera Toxin; D011392:Proline; C055247:N-acetylproline