Molecular Recognition through Isosteric
Interaction――Implication from Studies on Insulin
ZHANG You-Shang*, FENG You-Min, Guy G.DODSON1
(State Key Laboratory of Molecular Biology, Shanghai Institute of
Biochemistry,
Shanghai Institutes for Biological Sciences, the Chinese Academy of
Sciences, Shanghai 200031, China；
1Department of Chemistry,
University of York, York YO1 5DD, UK)
Abstract The
structural basis of molecular recognition in proteins is the specific three
dimensional structure or folding of the proteins, the information for which is
contained in the sequence. When the structural homology of proteins with known
or unknown functions are compared, it is an usual way to base such comparisons
on the hydrophobicity or hydrophilicity of the amino acid residues. Studies on
insulin by site directed mutagenesis reveal the importance of “isosteric
interaction” in considering the possible protein homology. With the
concept of “isosteric interaction” in mind there will be more to consider
for the structure and function studies on proteins and more choices for the
preparation of peptide and protein analogues or mimetics in pharmaceutical
industry.
Key words molecular recognition； isosteric interaction； structural homology； insulin
Received: November 5,
1999 Accepted: November 10, 1999
* Corresponding author: Tel, 86-21-64374430; Fax, 86-21-64338357; e-mail, [email protected]