NMR STRUCTURE OF HUMAN INSULIN MUTANT HIS-B10-ASP, VAL-B12-ABA, PRO-B28-LYS, LYS-B29-PRO, 15 STRUCTURES
How Insulin Binds: the B-Chain alpha-Helix Contacts the L1 beta-Helix of the Insulin Receptor.
MUTATIONAL ANALYSIS OF INVARIANT VALINE B12 IN INSULIN: IMPLICATION FOR RECEPTOR BINDING
STUDIES ON RECEPTOR BINDING SITE OF INSULIN: THE HYDROPHOBIC B12VALCAN BE SUBSTITUTED BY HYDROPHILIC THR
STERIC REQUIRMENTS AT POSITION B12 FOR HIGH BIOLOGICAL ACTIVITY IN INSULIN
[12-ASPARAGINE-B] HUMAN INSULIN. AN ANALOGUE WITH MODIFICATION IN THEHYDROPHOBIC CORE OF INSULIN
HIS-B10-ASP, VAL-B12-ABA, PRO-B28-LYS, LYS-B29-PRO
PARENT MOLECULE OF THIS DEPOSITION, CONTAINS THREE SUBSTITUTIONS
THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS(HUMAN)
This structure was determined by using standard 2D homonuclear techniques
the structures are based on a total of 590 restraints: 527 are NOE-derived distance constraints, 39 are dihedral angle restraints, 24 are hydrogen bond restraints.
DISTANCE GEOMETRY AND SIMULATED ANNEALING
1.2 mM ABA-B12-DKP-insulin, 90% H2O, 10% D2O
Aba-B12-DKP-insulin, protein unfolding, insulin receptor, receptor binding, HORMONE-GROWTH FACTOR COMPLEX