Structural analysis of the stable form of fibroblast growth factor 2 – FGF2-STAB
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F24%3A00600247" target="_blank" >RIV/61388963:_____/24:00600247 - isvavai.cz</a>
Alternative codes found
RIV/00216224:14310/24:00138632 RIV/00159816:_____/24:00081429
Result on the web
<a href="https://doi.org/10.1016/j.yjsbx.2024.100112" target="_blank" >https://doi.org/10.1016/j.yjsbx.2024.100112</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.yjsbx.2024.100112" target="_blank" >10.1016/j.yjsbx.2024.100112</a>
Alternative languages
Result language
angličtina
Original language name
Structural analysis of the stable form of fibroblast growth factor 2 – FGF2-STAB
Original language description
Fibroblast growth factor 2 (FGF2) is a signaling protein that plays a significant role in tissue development and repair. FGF2 binds to fibroblast growth factor receptors (FGFRs) alongside its co-factor heparin, which protects FGF2 from degradation. The binding between FGF2 and FGFRs induces intracellular signaling pathways such as RAS-MAPK, PI3K-AKT, and STAT. FGF2 has strong potential for application in cell culturing, wound healing, and cosmetics but the potential is severely limited by its low protein stability. The thermostable variant FGF2-STAB was constructed by computer-assisted protein engineering to overcome the natural limitation of FGF2. Previously reported characterization of FGF2-STAB revealed an enhanced ability to induce MAP/ERK signaling while having a lower dependence on heparin when compared with FGF2-wt. Here we report the crystal structure of FGF2-STAB solved at 1.3 Å resolution. Protein stabilization is achieved by newly formed hydrophobic interactions, polar contacts, and one additional hydrogen bond. The overall structure of FGF2-STAB is similar to FGF2-wt and does not reveal information on the experimentally observed lower dependence on heparin. A noticeable difference in flexibility in the receptor binding region can explain the differences in signaling between FGF2-STAB and its wild-type counterpart. Our structural analysis provided molecular insights into the stabilization and unique biological properties of FGF2-STAB.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
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
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Structural Biology: X
ISSN
2590-1524
e-ISSN
2590-1524
Volume of the periodical
10
Issue of the periodical within the volume
December
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
8
Pages from-to
100112
UT code for WoS article
001344373200001
EID of the result in the Scopus database
2-s2.0-85207035924