1DEI

DESHEPTAPEPTIDE (B24-B30) INSULIN

Summary for 1DEI

• Entry DOI: 10.2210/pdb1dei/pdb
• Descriptor: INSULIN (3 entities in total)
• Functional Keywords: hormone, glucose metabolism
• Biological source: Sus scrofa (pig); More
• Cellular location: Secreted: P01315
• Total number of polymer chains: 4
• Total formula weight: 9863.25

Authors

Bao, S.-J.,Chang, W.-R.,Wan, Z.-L.,Zhang, J.-P.,Liang, D.-C. (deposition date: 1996-05-15, release date: 1997-06-16, Last modification date: 2024-11-13)

Primary citation

Bao, S.J.,Xie, D.L.,Zhang, J.P.,Chang, W.R.,Liang, D.C.
Crystal structure of desheptapeptide(B24-B30)insulin at 1.6 A resolution: implications for receptor binding.
Proc.Natl.Acad.Sci.USA, 94:2975-2980, 1997

PubMed Abstract: 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.

PubMed: 9096331
DOI: 10.1073/pnas.94.7.2975

Experimental method

X-RAY DIFFRACTION (1.6 Å)