View source for 1dei


==DESHEPTAPEPTIDE (B24-B30) INSULIN==
<StructureSection load='1dei' size='340' side='right' caption='[[1dei]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dei]] is a 4 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DEI FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dei OCA], [http://pdbe.org/1dei PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dei RCSB], [http://www.ebi.ac.uk/pdbsum/1dei PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dei ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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 ==
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.

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>

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==
*[[Molecular Playground/Insulin|Molecular Playground/Insulin]]
== References ==
<references/>
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</StructureSection>
[[Category: Bao, S J]]
[[Category: Chang, W R]]
[[Category: Liang, D C]]
[[Category: Wan, Z L]]
[[Category: Zhang, J P]]
[[Category: Glucose metabolism]]
[[Category: Hormone]]