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Insulin binding to its receptor leads to negatively cooperative interactions among the receptor sites. Studies with 29 insulin analogues (animal insulins and proinsulin, insulin-like growth factor and chemically modified insulins) which vary 1,000-fold in their affinity for the receptor and in their biological potency, suggest that a discrete invariable region on the surface of the insulin monomer is responsible for including the negative cooperativity. This domain comprises some of the eight carboxy-terminal residues of the B-chain and the A21 asparagine. Burying of this 'cooperative site' in the dimerisation of insulin leads to a loss of negative cooperativity. A revised mapping of the insulin molecule is proposed, featuring distinct bioactive and cooperative sites.
P De Meyts, and
E Van Obberghen, and
J Roth
May 1986,
Biochemical and biophysical research communications,
P De Meyts, and
E Van Obberghen, and
J Roth
February 1981,
Nature,
P De Meyts, and
E Van Obberghen, and
J Roth
August 1977,
The Journal of biological chemistry,
P De Meyts, and
E Van Obberghen, and
J Roth
May 1980,
Journees annuelles de diabetologie de l'Hotel-Dieu,
P De Meyts, and
E Van Obberghen, and
J Roth
November 1994,
Molecular endocrinology (Baltimore, Md.),
P De Meyts, and
E Van Obberghen, and
J Roth
February 1976,
Nature,
P De Meyts, and
E Van Obberghen, and
J Roth
January 1975,
Biochemical and biophysical research communications,
P De Meyts, and
E Van Obberghen, and
J Roth
July 1994,
Endocrinology,
P De Meyts, and
E Van Obberghen, and
J Roth
May 1976,
Biochimica et biophysica acta,
P De Meyts, and
E Van Obberghen, and
J Roth
August 2010,
Cell,
