title: Closing in on a mechanism for activation.
abstract: When insulin-like growth factor-1 (IGF1) binds to its receptor, a physical constraint is released that allows the two transmembrane helices to come together to facilitate activation of the receptor.
authors.affiliation: Stevan R Hubbard is in the Kimmel Center for Biology and Medicine at the Skirball Institute and the Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, United States stevan.hubbard@med.nyu.edu.
authors.forename: Stevan R
authors.initials: SR
authors.lastname: Hubbard
authors.affiliation: W Todd Miller is in the Department of Physiology and Biophysics, Stony Brook University, Stony Brook, United States todd.miller@stonybrook.edu.
authors.forename: W Todd
authors.initials: WT
authors.lastname: Miller
mesh_terms: D019943:Amino Acid Substitution; D006801:Humans; D007328:Insulin / Q000378:metabolism; D007334:Insulin-Like Growth Factor I / Q000378:metabolism*; D008954:Models, Biological; D017526:Receptor, IGF Type 1 / Q000378:metabolism*; D011972:Receptor, Insulin / Q000378:metabolism
chemical_list: D007328:Insulin; D007334:Insulin-Like Growth Factor I; D017526:Receptor, IGF Type 1; D011972:Receptor, Insulin
keywords: FRET; IGF1 receptor; biochemistry; biophysics; human; kinetics; mechanism; structural biology