1dei: Difference between revisions
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<StructureSection load='1dei' size='340' side='right' caption='[[1dei]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1dei' size='340' side='right' caption='[[1dei]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dei]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1dei]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. 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://www.rcsb.org/pdb/explore.do?structureId=1dei RCSB], [http://www.ebi.ac.uk/pdbsum/1dei PDBsum]</span></td></tr> | </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]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1dei" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Pig]] | ||
[[Category: Bao, S J]] | [[Category: Bao, S J]] | ||
[[Category: Chang, W R]] | [[Category: Chang, W R]] | ||
Revision as of 17:17, 10 September 2015
DESHEPTAPEPTIDE (B24-B30) INSULINDESHEPTAPEPTIDE (B24-B30) INSULIN
Structural highlights
Function[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. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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