1dei

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Image:1dei.jpg

1dei, resolution 1.6Å

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DESHEPTAPEPTIDE (B24-B30) INSULIN

Overview

The crystal structure of desheptapeptide (B24-B30) insulin (DHPI), a, virtually inactive analog of insulin, was determined at 1.6 A resolution., In the refined structure model, DHPI retains three alpha-helices (A1-A8, A12-A18, and B9-B19) as its structural framework, while great, conformational changes occur in the N and C termini of B-chain. The, beta-turn, which lies in B20-B30 in insulin and insulin analogs with high, potency, no longer exists in DHPI. Relative motion is observed among the, three alpha-helices, each as a rigid functional group. In contrast, a, region covering B5-B6 and A6-A11 exhibits a relatively stable, conformation. We interpret our results as identifying: (i) the importance, of beta-turn in determining the receptor-binding potency of insulin and, (ii) a leading role of PheB24 in maintaining the beta-turn structure.

About this Structure

1DEI is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Crystal structure of desheptapeptide(B24-B30)insulin at 1.6 A resolution: implications for receptor binding., Bao SJ, Xie DL, Zhang JP, Chang WR, Liang DC, Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):2975-80. PMID:9096331

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