In:
Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 94, No. 7 ( 1997-04), p. 2975-2980
Abstract:
The crystal structure of desheptapeptide (B24–B30) insulin (DHPI), a virtually inactive analog of insulin, was determined at 1.6 Å resolution. In the refined structure model, DHPI retains three α-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 β-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 α-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 β-turn in determining the receptor-binding potency of insulin and ( ii ) a leading role of Phe B24 in maintaining the β-turn structure.
Type of Medium:
Online Resource
ISSN:
0027-8424
,
1091-6490
DOI:
10.1073/pnas.94.7.2975
Language:
English
Publisher:
Proceedings of the National Academy of Sciences
Publication Date:
1997
detail.hit.zdb_id:
209104-5
detail.hit.zdb_id:
1461794-8
SSG:
11
SSG:
12
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