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1dei

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{{STRUCTURE_1dei| PDB=1dei | SCENE= }}
{{STRUCTURE_1dei| PDB=1dei | SCENE= }}
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'''DESHEPTAPEPTIDE (B24-B30) INSULIN'''
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===DESHEPTAPEPTIDE (B24-B30) INSULIN===
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==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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9096331 is the PubMed ID number.
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:45:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:54:25 2008''

Revision as of 19:54, 30 June 2008

Image:1dei.png

Template:STRUCTURE 1dei

DESHEPTAPEPTIDE (B24-B30) INSULIN

Template:ABSTRACT PUBMED 9096331

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

Page seeded by OCA on Mon Jun 30 22:54:25 2008

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