1dei: Difference between revisions
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'''DESHEPTAPEPTIDE (B24-B30) INSULIN''' | {{Structure | ||
|PDB= 1dei |SIZE=350|CAPTION= <scene name='initialview01'>1dei</scene>, resolution 1.6Å | |||
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|LIGAND= | |||
|ACTIVITY= | |||
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'''DESHEPTAPEPTIDE (B24-B30) INSULIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DEI is a [ | 1DEI is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEI OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9096331 9096331] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: hormone]] | [[Category: hormone]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:37:18 2008'' |
Revision as of 11:37, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
DESHEPTAPEPTIDE (B24-B30) INSULIN
OverviewOverview
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 StructureAbout this Structure
1DEI is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.
ReferenceReference
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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