scholarly journals Mechanisms of allosteric and mixed mode aromatase inhibitors

2021 ◽  
Author(s):  
Samson A. Souza ◽  
Abby Held ◽  
Wenjie J. Lu ◽  
Brendan Drouhard ◽  
Bryant Avila ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Aromatase Inhibitors ◽  
Binding Sites ◽  
Mixed Mode ◽  
Ligand Binding Sites ◽  
Multiple Ligand

Identification of multiple ligand binding sites in aromatase.

Multiple ligand binding sites on domain seven of human complement factor H

2001 ◽  
Vol 1 (3) ◽  
pp. 433-443 ◽  
Author(s):  
Eleni Giannakis ◽  
Dean A. Male ◽  
Rebecca J. Ormsby ◽  
Carolyn Mold ◽  
T.Sakari Jokiranta ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Binding Sites ◽  
Factor H ◽  
Complement Factor H ◽  
Complement Factor ◽  
Human Complement ◽  
Ligand Binding Sites ◽  
Multiple Ligand

scholarly journals Multiple ligand binding sites regulate the Hedgehog signal transducer Smoothened in vertebrates

2018 ◽  
Vol 51 ◽  
pp. 81-88 ◽  
Author(s):  
Eamon FX Byrne ◽  
Giovanni Luchetti ◽  
Rajat Rohatgi ◽  
Christian Siebold
Keyword(s):  
Ligand Binding ◽  
Binding Sites ◽  
Signal Transducer ◽  
Ligand Binding Sites ◽  
Multiple Ligand ◽  
Hedgehog Signal

scholarly journals Avidity observed between a bivalent inhibitor and an enzyme monomer with a single active site

PLoS ONE ◽  
2021 ◽  
Vol 16 (11) ◽  
pp. e0249616
Author(s):  
Shiran Lacham-Hartman ◽  
Yulia Shmidov ◽  
Evette S. Radisky ◽  
Ronit Bitton ◽  
David B. Lukatsky ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Binding Affinity ◽  
Protein Interactions ◽  
Protein Complex ◽  
Binding Sites ◽  
Protein Protein Interactions ◽  
Multiple Receptors ◽  
Ligand Binding Sites ◽  
Multiple Ligands ◽  
Multiple Ligand

Although myriad protein–protein interactions in nature use polyvalent binding, in which multiple ligands on one entity bind to multiple receptors on another, to date an affinity advantage of polyvalent binding has been demonstrated experimentally only in cases where the target receptor molecules are clustered prior to complex formation. Here, we demonstrate cooperativity in binding affinity (i.e., avidity) for a protein complex in which an engineered dimer of the amyloid precursor protein inhibitor (APPI), possessing two fully functional inhibitory loops, interacts with mesotrypsin, a soluble monomeric protein that does not self-associate or cluster spontaneously. We found that each inhibitory loop of the purified APPI homodimer was over three-fold more potent than the corresponding loop in the monovalent APPI inhibitor. This observation is consistent with a suggested mechanism whereby the two APPI loops in the homodimer simultaneously and reversibly bind two corresponding mesotrypsin monomers to mediate mesotrypsin dimerization. We propose a simple model for such dimerization that quantitatively explains the observed cooperativity in binding affinity. Binding cooperativity in this system reveals that the valency of ligands may affect avidity in protein–protein interactions including those of targets that are not surface-anchored and do not self-associate spontaneously. In this scenario, avidity may be explained by the enhanced concentration of ligand binding sites in proximity to the monomeric target, which may favor rebinding of the multiple ligand binding sites with the receptor molecules upon dissociation of the protein complex.

Maghemite nanoparticles coated with human serum albumin: combining targeting by the iron-acquisition pathway and potential in photothermal therapies

2017 ◽  
Vol 5 (17) ◽  
pp. 3154-3162 ◽  
Author(s):  
J. Hai ◽  
H. Piraux ◽  
E. Mazarío ◽  
J. Volatron ◽  
N. T. Ha-Duong ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Ligand Binding ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Iron Acquisition ◽  
Maghemite Nanoparticles ◽  
Ligand Binding Sites ◽  
Transport Vehicle ◽  
Multiple Ligand

Human serum albumin (HSA), the most abundant plasma protein in human blood, is a natural transport vehicle with multiple ligand binding sites.

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