Hydrophobic Amino Acids as Universal Elements of Protein-Induced DNA Structure Deformation
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F20%3A00531026" target="_blank" >RIV/61388963:_____/20:00531026 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/20:10422524
Result on the web
<a href="https://www.mdpi.com/1422-0067/21/11/3986" target="_blank" >https://www.mdpi.com/1422-0067/21/11/3986</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/ijms21113986" target="_blank" >10.3390/ijms21113986</a>
Alternative languages
Result language
angličtina
Original language name
Hydrophobic Amino Acids as Universal Elements of Protein-Induced DNA Structure Deformation
Original language description
Interaction with the DNA minor groove is a significant contributor to specific sequence recognition in selected families of DNA-binding proteins. Based on a statistical analysis of 3D structures of protein–DNA complexes, we propose that distortion of the DNA minor groove resulting from interactions with hydrophobic amino acid residues is a universal element of protein–DNA recognition. We provide evidence to support this by associating each DNA minor groove-binding amino acid residue with the local dimensions of the DNA double helix using a novel algorithm. The widened DNA minor grooves are associated with high GC content. However, some AT-rich sequences contacted by hydrophobic amino acids (e.g., phenylalanine) display extreme values of minor groove width as well. For a number of hydrophobic amino acids, distinct secondary structure preferences could be identified for residues interacting with the widened DNA minor groove. These results hold even after discarding the most populous families of minor groove-binding proteins.
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
<a href="/en/project/EF16_019%2F0000729" target="_blank" >EF16_019/0000729: Chemical biology for drugging undruggable targets</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
International Journal of Molecular Sciences
ISSN
1422-0067
e-ISSN
—
Volume of the periodical
21
Issue of the periodical within the volume
11
Country of publishing house
CH - SWITZERLAND
Number of pages
15
Pages from-to
3986
UT code for WoS article
000543400300248
EID of the result in the Scopus database
2-s2.0-85085927020