Protein heterodimerization through ligand-bridged multivalent pre-organization: enhancing ligand binding toward both protein targets.
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.
Liu
Jiyun
J
Biomolecular Structure Center, Department of Chemistry, University of Washington, Seattle, Washington 98195, USA.
Zhang
Zhongsheng
Z
Tan
Xiaojian
X
Hol
Wim G J
WG
Verlinde
Christophe L M J
CL
Fan
Erkang
E
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
D008024:Ligands; D000683:Serum Amyloid P-Component; D002772:Cholera Toxin; D011392:Proline; C055247:N-acetylproline