1dei

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(New page: 200px<br /><applet load="1dei" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dei, resolution 1.6&Aring;" /> '''DESHEPTAPEPTIDE (B24-...)
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[[Image:1dei.jpg|left|200px]]<br /><applet load="1dei" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dei, resolution 1.6&Aring;" />
 
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'''DESHEPTAPEPTIDE (B24-B30) INSULIN'''<br />
 
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==Overview==
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==DESHEPTAPEPTIDE (B24-B30) INSULIN==
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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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<StructureSection load='1dei' size='340' side='right'caption='[[1dei]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dei]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DEI FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dei OCA], [https://pdbe.org/1dei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dei RCSB], [https://www.ebi.ac.uk/pdbsum/1dei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dei ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/INS_PIG INS_PIG] Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
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==About this Structure==
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==See Also==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DEI OCA].
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*[[Insulin 3D Structures|Insulin 3D Structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Bao, S.J.]]
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[[Category: Bao S-J]]
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[[Category: Chang, W.R.]]
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[[Category: Chang W-R]]
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[[Category: Liang, D.C.]]
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[[Category: Liang D-C]]
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[[Category: Wan, Z.L.]]
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[[Category: Wan Z-L]]
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[[Category: Zhang, J.P.]]
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[[Category: Zhang J-P]]
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[[Category: glucose metabolism]]
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[[Category: hormone]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:13:05 2007''
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Current revision

DESHEPTAPEPTIDE (B24-B30) INSULIN

PDB ID 1dei

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