Mutations at hypothetical binding site 2 in insulin and insulin-like growth factors 1 and 2
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F23%3A00575692" target="_blank" >RIV/61388963:_____/23:00575692 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.1016/bs.vh.2023.01.010" target="_blank" >https://doi.org/10.1016/bs.vh.2023.01.010</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/bs.vh.2023.01.010" target="_blank" >10.1016/bs.vh.2023.01.010</a>
Alternative languages
Result language
angličtina
Original language name
Mutations at hypothetical binding site 2 in insulin and insulin-like growth factors 1 and 2
Original language description
Elucidating how insulin and the related insulin-like growth factors 1 and 2 (IGF-1 and IGF-2) bind to their cellular receptors (IR and IGF-1R) and how the receptors are activated has been the holy grail for generations of scientists. However, deciphering the 3D structure of tyrosine kinase receptors and their hormone-bound complexes has been complicated by the flexible and dimeric nature of the receptors and the dynamic nature of their interaction with hormones. Therefore, mutagenesis of hormones and kinetic studies first became an important tool for studying receptor interactions. It was suggested that hormones could bind to receptors through two binding sites on the hormone surface called site 1 and site 2. A breakthrough in knowledge came with the solution of cryoelectron microscopy (cryoEM) structures of hormone-receptor complexes. In this chapter, we document in detail the mutagenesis of insulin, IGF-1, and IGF-2 with emphasis on modifications of the hypothetical binding site 2 in the hormones, and we discuss the results of structure-activity studies in light of recent cryoEM structures of hormone complexes with IR and IGF-1R.
Czech name
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Czech description
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Classification
Type
C - Chapter in a specialist book
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
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
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Book/collection name
Hormone Receptors: Structures and Functions
ISBN
978-0-443-13455-5
Number of pages of the result
44
Pages from-to
187-230
Number of pages of the book
662
Publisher name
Elsevier
Place of publication
Cambridge
UT code for WoS chapter
001101822300007