Identification of a Cd2+- and Zn2+-Binding Site in CytochromecUsing FTIR Coupled to an ATR Microdialysis Setup and NMR Spectroscopy†

Biochemistry ◽  
2005 ◽  
Vol 44 (24) ◽  
pp. 8652-8663 ◽  
Author(s):  
Samuel Gourion-Arsiquaud ◽  
Soizic Chevance ◽  
Pierre Bouyer ◽  
Lionel Garnier ◽  
J.-L. Montillet ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Binding Site

Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy

2005 ◽  
Vol 12 (3) ◽  
pp. 451-456 ◽  
Author(s):  
Lars Briese ◽  
Andrea Preusser ◽  
Dieter Willbold
Keyword(s):  
Nmr Spectroscopy ◽  
Binding Site ◽  
Full Length ◽  
Hiv 1

scholarly journals KRAS is vulnerable to reversible switch-II pocket engagement in cells

2021 ◽  
Author(s):  
James D Vasta ◽  
D. Matthew Peacock ◽  
Qinheng Zheng ◽  
Joel A Walker ◽  
Ziyang Zhang ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Binding Site ◽  
Small Molecule ◽  
Therapeutic Approach ◽  
Small Molecule Inhibitors ◽  
Drug Binding ◽  
Gtp Hydrolysis ◽  
Drug Binding Site ◽  
Covalent Ligands ◽  
P Ligands

Current small molecule inhibitors of KRAS (G12C) bind irreversibly in the switch-II pocket, exploiting the strong nucleophilicity of the acquired cysteine as well as the preponderance of the GDP-bound form of this mutant. Nevertheless, many oncogenic KRAS mutants lack these two features, and it remains unknown whether targeting the switch-II pocket is a practical therapeutic approach for KRAS mutants beyond G12C. Here we use NMR spectroscopy and a novel cellular KRAS engagement assay to address this question by examining a collection of SII-P ligands from the literature and from our own laboratory. We show that the switch-II pockets of many GTP hydrolysis-deficient KRAS hotspot (G12, G13, Q61) mutants are accessible using non-covalent ligands, and that this accessibility is not necessarily coupled to the GDP state of KRAS. The results we describe here emphasize the switch-II pocket as a privileged drug binding site on KRAS and unveil new therapeutic opportunities in RAS-driven cancer.

Identification of the barstar binding site of barnase by NMR spectroscopy and hydrogen-deuterium exchange

FEBS Letters ◽  
1993 ◽  
Vol 331 (1-2) ◽  
pp. 165-172 ◽  
Author(s):  
David N.M. Jones ◽  
Mark Bycroft ◽  
Michael J. Lubienski ◽  
Alan R. Fersht
Keyword(s):  
Nmr Spectroscopy ◽  
Binding Site ◽  
Deuterium Exchange ◽  
Hydrogen Deuterium Exchange ◽  
Hydrogen Deuterium

A Chimeric GPCR Model Mimicking the Ligand Binding Site of the Human Y1 Receptor Studied by NMR Spectroscopy

ChemBioChem ◽  
2011 ◽  
Vol 12 (11) ◽  
pp. 1690-1693 ◽  
Author(s):  
Reto Walser ◽  
Jörg H. Kleinschmidt ◽  
Oliver Zerbe
Keyword(s):  
Nmr Spectroscopy ◽  
Ligand Binding ◽  
Binding Site ◽  
Ligand Binding Site ◽  
Y1 Receptor

scholarly journals Selective Interface Detection:  Mapping Binding Site Contacts in Membrane Proteins by NMR Spectroscopy

2005 ◽  
Vol 127 (16) ◽  
pp. 5734-5735 ◽  
Author(s):  
Suzanne R. Kiihne ◽  
Alain F. L. Creemers ◽  
Willem J. de Grip ◽  
Petra H. M. Bovee-Geurts ◽  
Johan Lugtenburg ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Membrane Proteins ◽  
Binding Site

Molecular Recognition of Rosmarinic Acid fromSalvia sclareoidesExtracts by Acetylcholinesterase: A New Binding Site Detected by NMR Spectroscopy

2013 ◽  
Vol 19 (21) ◽  
pp. 6641-6649 ◽  
Author(s):  
Filipa Marcelo ◽  
Catarina Dias ◽  
Alice Martins ◽  
Paulo J. Madeira ◽  
Tiago Jorge ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Molecular Recognition ◽  
Binding Site ◽  
Rosmarinic Acid
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