View source for 6kha


==Solution structure of bovine insulin amyloid intermediate-2==
<StructureSection load='6kha' size='340' side='right'caption='[[6kha]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6kha]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KHA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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=6kha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kha OCA], [https://pdbe.org/6kha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kha RCSB], [https://www.ebi.ac.uk/pdbsum/6kha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kha ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Insulin has long served as a model for protein aggregation, both due to the importance of aggregation in the manufacture of insulin and because the structural biology of insulin has been extensively characterized. Despite intensive study, details about the initial triggers for aggregation have remained elusive at the molecular level. We show here that at acidic pH the aggregation of insulin is likely initiated by a partially folded monomeric intermediate. High resolution structures of the partially folded intermediate show that it is coarsely similar to the initial monomeric structure but differs in subtle details - the A chain helices on the receptor interface are more disordered and the B chain helix is displaced from the from C-terminal A chain helix when compared to the stable monomer. The result of these movements is the creation of a hydrophobic cavity in the center of the protein that may serve as nucleation site for oligomer formation. Knowledge of this transition may aid in the engineering of insulin variants that retain the favorable pharamacokinetic properties of monomeric insulin but are more resistant to aggregation. This article is protected by copyright. All rights reserved.

High Resolution Structure of A Partially Folded Insulin Aggregation Intermediate.,Ratha BN, Kar RK, Brender JR, Pariary R, Sahoo B, Kalita S, Bhunia A Proteins. 2020 Jul 18. doi: 10.1002/prot.25983. PMID:32683793<ref>PMID:32683793</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 6kha" style="background-color:#fffaf0;"></div>

==See Also==
*[[Insulin 3D Structures|Insulin 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Bhunia A]]
[[Category: Brender JB]]
[[Category: Kar RK]]
[[Category: Ratha BN]]