1dei: Difference between revisions

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[[Image:1dei.jpg|left|200px]]
{{Seed}}
[[Image:1dei.png|left|200px]]


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{{STRUCTURE_1dei|  PDB=1dei  |  SCENE=  }}  
{{STRUCTURE_1dei|  PDB=1dei  |  SCENE=  }}  


'''DESHEPTAPEPTIDE (B24-B30) INSULIN'''
===DESHEPTAPEPTIDE (B24-B30) INSULIN===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_9096331}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_9096331}}


==About this Structure==
==About this Structure==
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[[Category: Glucose metabolism]]
[[Category: Glucose metabolism]]
[[Category: Hormone]]
[[Category: Hormone]]
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