Exploration of the supramolecular interactions involving tris-dipicolinate lanthanide complexes in protein crystals by a combined biostructural, computational and NMR study.
Incorporating in a non-covalent manner lanthanide derivatives into protein crystals has shown to be of prime interest for X-ray crystallography, insofar as these versatile compounds can co-crystallize with proteins through supramolecular interactions, in addition to being strong anomalous scatterers for anomalous-based diffraction techniques. In this paper, the selective affinity of tris-dipicolinate lanthanide complexes for cationic amino-acid residues is explored, using a panel of experimental (X-ray diffraction, NMR titration) and theoretical methods that provides access to an accurate description of the interaction process.
Laboratoire de Chimie, UMR 5182 CNRS - ENS-Lyon, 46 allée d'Italie, 69364 Lyon cedex 07, France. olivier.maury@ens-lyon.fr.
Elise
E
Dumont
Guillaume
G
Pompidor
Anthony
A
D'Aléo
Jean
J
Vicat
Loïc
L
Toupet
Richard
R
Kahn
Eric
E
Girard
Olivier
O
Maury
Nicolas
N
Giraud
D056831:Coordination Complexes / Q000737:chemistry*; D018360:Crystallography, X-Ray; D028581:Lanthanoid Series Elements / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010848:Picolinic Acids / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D014503:Urate Oxidase / Q000737:chemistry / Q000378:metabolism
D056831:Coordination Complexes; D028581:Lanthanoid Series Elements; D010848:Picolinic Acids; D010940:Plant Proteins; D011506:Proteins; C057542:thaumatin II protein, Thaumatococcus daniellii; D014503:Urate Oxidase; C004860:dipicolinic acid