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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

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

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

  • 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