Competition between Drugs and Nutrients for Specific Ligand Binding Sites on Human Serum Albumin1

2015 ◽  
pp. 179-182 ◽  
Author(s):  
E. Kiem ◽  
K. J. Fehske ◽  
W. E. M�ller
Keyword(s):  
Ligand Binding ◽  
Human Serum ◽  
Binding Sites ◽  
Ligand Binding Sites ◽  
Specific Ligand

scholarly journals Differential Effects of Methoxy Group on the Interaction of Curcuminoids with Two Major Ligand Binding Sites of Human Serum Albumin

PLoS ONE ◽  
2014 ◽  
Vol 9 (2) ◽  
pp. e87919 ◽  
Author(s):  
Hiroki Sato ◽  
Victor Tuan Giam Chuang ◽  
Keishi Yamasaki ◽  
Noriyuki Yamaotsu ◽  
Hiroshi Watanabe ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Ligand Binding ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Methoxy Group ◽  
Differential Effects ◽  
Ligand Binding Sites

scholarly journals Ligand-Binding Sites in Human Serum Amyloid P Component

1996 ◽  
Vol 239 (3) ◽  
pp. 850-856 ◽  
Author(s):  
Niels H. H. Heegaard ◽  
Peter M. H. Heegaard ◽  
Peter Roepstorff ◽  
Frank A. Robey
Keyword(s):  
Ligand Binding ◽  
Human Serum ◽  
Binding Sites ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Ligand Binding Sites ◽  
Amyloid P

scholarly journals Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle

2021 ◽  
Vol 7 (22) ◽  
pp. eabg4474
Author(s):  
Michael Rohde ◽  
Konstantin Laun ◽  
Ingo Zebger ◽  
Sven T. Stripp ◽  
Oliver Einsle
Keyword(s):  
Ligand Binding ◽  
Binding Sites ◽  
Strong Field ◽  
Bound State ◽  
Ligand Binding Sites ◽  
Hydrocarbon Formation ◽  
Co Reduction ◽  
Biological Nitrogen ◽  
Access Pathway ◽  
Specific Ligand

Besides its role in biological nitrogen fixation, vanadium-containing nitrogenase also reduces carbon monoxide (CO) to hydrocarbons, in analogy to the industrial Fischer-Tropsch process. The protein yields 93% of ethylene (C2H4), implying a C–C coupling step that mandates the simultaneous binding of two CO at the active site FeV cofactor. Spectroscopic data indicated multiple CO binding events, but structural analyses of Mo and V nitrogenase only confirmed a single site. Here, we report the structure of a two CO-bound state of V nitrogenase at 1.05 Å resolution, with one μ-bridging and one terminal CO molecule. This additional, specific ligand binding site suggests a mechanistic route for CO reduction and hydrocarbon formation, as well as a second access pathway for protons required during the reaction. Moreover, carbonyls are strong-field ligands that are chemically similar to mechanistically relevant hydrides that may be formed and used in a fully analogous fashion.

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.

scholarly journals Diversity in the structures and ligand-binding sites of nematode fatty acid and retinol-binding proteins revealed by Na-FAR-1 from Necator americanus

2015 ◽  
Vol 471 (3) ◽  
pp. 403-414 ◽  
Author(s):  
M. Florencia Rey-Burusco ◽  
Marina Ibáñez-Shimabukuro ◽  
Mads Gabrielsen ◽  
Gisela R. Franchini ◽  
Andrew J. Roe ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Ligand Binding ◽  
Tissue Distribution ◽  
Binding Sites ◽  
Binding Proteins ◽  
Retinol Binding Protein ◽  
Internal Cavity ◽  
Binding Characteristics ◽  
Necator Americanus ◽  
Ligand Binding Sites

Necator americanus fatty acid and retinol-binding protein-1 (Na-FAR-1) is an abundantly expressed FAR from a parasitic hookworm. The present work describes its tissue distribution, structure and ligand-binding characteristics and shows that Na-FAR-1 expands to transport multiple FA molecules in its internal cavity.

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