title: Closed form of liganded glutamine-binding protein by rotational-echo double-resonance NMR.
abstract: Rotational-echo double-resonance NMR has been used to determine internuclear distances in the complex of glutamine-binding protein and its ligand, l-glutamine. The distances between the ligand and Tyr185 are consistent with the results of molecular dynamics simulations constrained by three REDOR-determined distances to His156. This model is also consistent with six other REDOR-determined internuclear distances, most of which agree with values from the first report of an X-ray structure of the complex of glutamine-binding protein and l-glutamine.
authors.affiliation: Department of Chemistry, Washington University, St. Louis, Missouri 63130, USA.
authors.forename: C A
authors.initials: CA
authors.lastname: Klug
authors.forename: K
authors.initials: K
authors.lastname: Tasaki
authors.forename: N
authors.initials: N
authors.lastname: Tjandra
authors.forename: C
authors.initials: C
authors.lastname: Ho
authors.forename: J
authors.initials: J
authors.lastname: Schaefer
mesh_terms: D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D005461:Fluorine; D005973:Glutamine / Q000378:metabolism*; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D014443:Tyrosine / Q000737:chemistry
chemical_list: D002352:Carrier Proteins; D008024:Ligands; C037853:glutamine transport proteins; D005973:Glutamine; D005461:Fluorine; D014443:Tyrosine