Key amino acid residues involved in multi-point binding interactions between brazzein, a sweet protein, and the T1R2-T1R3 human sweet receptor.
Assadi-Porter
Fariba M
FM
National Magnetic Resonance Facility at Madison, Biochemistry Department, University of Wisconsin-Madison, 433 Babcock Drive, Madison, WI 53706, USA. fariba@nmrfam.wisc.edu
Maillet
Emeline L
EL
Radek
James T
JT
Quijada
Jeniffer
J
Markley
John L
JL
Max
Marianna
M
D019943:Amino Acid Substitution / Q000235:genetics; D002460:Cell Line; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins / Q000235:genetics / Q000378:metabolism; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D025941:Protein Interaction Mapping; D020836:Protein Structure, Quaternary; D043562:Receptors, G-Protein-Coupled / Q000235:genetics / Q000378:metabolism*
D050505:Mutant Proteins; D010940:Plant Proteins; D043562:Receptors, G-Protein-Coupled; C090521:brazzein protein, Pentadiplandra brazzeana; C431926:taste receptors, type 1