1dei

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[[Image:1dei.jpg|left|200px]]<br /><applet load="1dei" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1dei.jpg|left|200px]]
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caption="1dei, resolution 1.6&Aring;" />
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'''DESHEPTAPEPTIDE (B24-B30) INSULIN'''<br />
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{{Structure
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|PDB= 1dei |SIZE=350|CAPTION= <scene name='initialview01'>1dei</scene>, resolution 1.6&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''DESHEPTAPEPTIDE (B24-B30) INSULIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9096331 9096331]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:37:18 2008''

Revision as of 08:37, 20 March 2008

Image:1dei.jpg


PDB ID 1dei

Drag the structure with the mouse to rotate
, resolution 1.6Å
Coordinates: save as pdb, mmCIF, xml



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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