1H[19F] NOE NMR structural signatures of the insulin R6 hexamer: evidence of a capped HisB10 site in aryl- and arylacryloyl-carboxylate complexes.
NEW AND IMPROVED INSULIN: 1H[19F] NOE NMR difference spectra for CF(3)-substituted aromatic carboxylates bound at the HisB10 sites of the R(6) human insulin (HI) hexamer show strong NOEs between the CF(3) groups and the LeuB6, AsnB3, and PheB1 sidechains. The NOEs and structural modeling establish that these carboxylates form closed complexes with the HisB10 site capped by the PheB1 rings.
Keidel
Donald
D
Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
Bonaccio
Maria
M
Ghaderi
Nima
N
Niks
Dimitri
D
Borchardt
Dan
D
Dunn
Michael F
MF
D002264:Carboxylic Acids / Q000737:chemistry*; D005461:Fluorine / Q000737:chemistry; D006639:Histidine / Q000737:chemistry*; D006801:Humans; D006859:Hydrogen / Q000737:chemistry; D007328:Insulin / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation
D002264:Carboxylic Acids; D007328:Insulin; D005461:Fluorine; D006639:Histidine; D006859:Hydrogen