BMB Reports
- 제33권2호
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- Pages.120-125
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- 2000
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- 1976-670X(eISSN)
Solution Structure of an Active Mini-Proinsulin, M2PI: Inter-chain Flexibility is Crucial for Insulin Activity
- Cho, Yoon-Sang (Structural Biology Center, Korea Institute of Science and Technology) ;
- Chang, Seung-Gu (the Hanhyo Institute of Technology) ;
- Choi, Ki-Doo (the Hanhyo Institute of Technology) ;
- Shin, Hang-Cheol (the Hanhyo Institute of Technology) ;
- Ahn, Byung-Yoon (the Graduate School of Biotechnology, Korea University) ;
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Kim, Key-Sun
(Structural Biology Center, Korea Institute of Science and Technology)
- 발행 : 2000.03.31
초록
M2PI is an active single chain mini-proinsulin with a 9-residue linker containing the turn-forming sequence 'YPGDV' between the B- and A-chains, but which retains about 50% of native insulin receptor binding activity. The refolding efficiency of M2PI is higher than proinsulin by 20-40% at alkaline pH, and native insulin is generated by the enzymatic conversion of M2PI. The solution structure of M2PI was determined by NMR spectroscopy. The global structure of M2PI is similar to that of native insulin, but the flexible linker between the B- and A-chains perturbed the N-terminal A-chain and C-terminal B-chain. The helix in the N-terminal A-chain is partly perturbed and the