Human insulin analogues modified at the B26 site reveal a hormone conformation that is undetected in the receptor complex
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F14%3A00435229" target="_blank" >RIV/61388963:_____/14:00435229 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1107/S1399004714017775" target="_blank" >http://dx.doi.org/10.1107/S1399004714017775</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1107/S1399004714017775" target="_blank" >10.1107/S1399004714017775</a>
Alternative languages
Result language
angličtina
Original language name
Human insulin analogues modified at the B26 site reveal a hormone conformation that is undetected in the receptor complex
Original language description
The structural characterization of the insulin-insulin receptor (IR) interaction still lacks the conformation of the crucial B21-B30 insulin region, which must be different from that in its storage forms to ensure effective receptor binding. Here, it isshown that insulin analogues modified by natural amino acids at the TyrB26 site can represent an active form of this hormone. In particular, [AsnB26]-insulin and [GlyB26]-insulin attain a B26-turn-like conformation that differs from that in all known structures of the native hormone. It also matches the receptor interface, avoiding substantial steric clashes. This indicates that insulin may attain a B26-turn-like conformation upon IR binding. Moreover, there is an unexpected, but significant, binding specificity of the AsnB26 mutant for predominantly the metabolic B isoform of the receptor. As it is correlated with the B26 bend of the B-chain of the hormone, the structures of AsnB26 analogues may provide the first structural insight int
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Acta Crystallographica Section D-Biological Crystallography
ISSN
0907-4449
e-ISSN
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Volume of the periodical
70
Issue of the periodical within the volume
10
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
2765-2774
UT code for WoS article
000343060900025
EID of the result in the Scopus database
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