Title : Structural integrity of the B24 site in human insulin is important for hormone functionality.

Pub. Date : 2013 Apr 12

PMID : 23447530






2 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The inactive [HisB24]-insulin molecule is remarkably rigid due to a tight accommodation of the L-His side chain in the B24 binding pocket that results in the stronger tethering of B25-B28 residues to the protein core. Histidine insulin Homo sapiens
2 In contrast, the highly active [D-HisB24]-insulin is more flexible, and the reverse chirality of the B24C(alpha) atom swayed the D-His(B24) side chain into the solvent. Histidine insulin Homo sapiens