1dei

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== Structural highlights ==
== Structural highlights ==
<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>
<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='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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</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>
</table>
</table>
== Function ==
== Function ==
[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.
[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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== Publication Abstract from PubMed ==
 
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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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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<ref>PMID:9096331</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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<div class="pdbe-citations 1dei" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Insulin 3D Structures|Insulin 3D Structures]]
*[[Insulin 3D Structures|Insulin 3D Structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

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DESHEPTAPEPTIDE (B24-B30) INSULIN

PDB ID 1dei

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