1dei: Difference between revisions
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[[ | ==DESHEPTAPEPTIDE (B24-B30) INSULIN== | ||
<StructureSection load='1dei' size='340' side='right' caption='[[1dei]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1dei]] is a 4 chain structure with sequence 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]. 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><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> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Molecular Playground/Insulin|Molecular Playground/Insulin]] | *[[Molecular Playground/Insulin|Molecular Playground/Insulin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Bao, S J.]] | [[Category: Bao, S J.]] | ||
Revision as of 09:28, 4 September 2014
DESHEPTAPEPTIDE (B24-B30) INSULINDESHEPTAPEPTIDE (B24-B30) INSULIN
Structural highlights
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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