1dei
From Proteopedia
(New page: 200px<br /><applet load="1dei" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dei, resolution 1.6Å" /> '''DESHEPTAPEPTIDE (B24-...) |
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| - | [[Image:1dei.jpg|left|200px]]<br /><applet load="1dei" size=" | + | [[Image:1dei.jpg|left|200px]]<br /><applet load="1dei" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dei, resolution 1.6Å" /> | caption="1dei, resolution 1.6Å" /> | ||
'''DESHEPTAPEPTIDE (B24-B30) INSULIN'''<br /> | '''DESHEPTAPEPTIDE (B24-B30) INSULIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of desheptapeptide (B24-B30) insulin (DHPI), a | + | 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 Structure== | ==About this Structure== | ||
| - | 1DEI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http:// | + | 1DEI is a [http://en.wikipedia.org/wiki/Protein_complex 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== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
| - | [[Category: Bao, S | + | [[Category: Bao, S J.]] |
| - | [[Category: Chang, W | + | [[Category: Chang, W R.]] |
| - | [[Category: Liang, D | + | [[Category: Liang, D C.]] |
| - | [[Category: Wan, Z | + | [[Category: Wan, Z L.]] |
| - | [[Category: Zhang, J | + | [[Category: Zhang, J P.]] |
[[Category: glucose metabolism]] | [[Category: glucose metabolism]] | ||
[[Category: hormone]] | [[Category: hormone]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:50 2008'' |
Revision as of 10:15, 21 February 2008
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DESHEPTAPEPTIDE (B24-B30) INSULIN
Overview
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 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
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