Title : Isosteric replacement of A3 Val of porcine insulin by allo-Thr.

Pub. Date : 2002 Jan

PMID : 12018409






5 Functional Relationships(s)
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1 Isosteric replacement of A3 Val of porcine insulin by allo-Thr. Threonine insulin Homo sapiens
2 When A3 Val was replaced by Thr, which is hydrophilic but isosteric with Val, substantial insulin activity was retained. Threonine insulin Homo sapiens
3 Here we report the replacement of A3 Val of porcine insulin by the unnatural allo-Thr. Threonine insulin Homo sapiens
4 The in vivo biological activity of A3 allo-Thr insulin is similar to that of A3 Thr insulin or native insulin, but its receptor binding activity is 7.6% instead of 50% for A3 Thr insulin, indicating that at the A3 position the hydrophilic OH group of Thr could be more tolerated in receptor binding than the OH group of allo-Thr. Threonine insulin Homo sapiens
5 The retention of insulin activity by substituting A3 Val with the unnatural isosteric allo-Thr demonstrates again the importance of isosteric interaction in the binding of insulin with its receptor. Threonine insulin Homo sapiens