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Wyszukujesz frazę "heparin-binding protein" wg kryterium: Temat


Wyświetlanie 1-2 z 2
Tytuł:
Azurocidin - inactive serine proteinase homolog acting as a multifunctional inflammatory mediator.
Autorzy:
Wątorek, Wiesław
Powiązania:
https://bibliotekanauki.pl/articles/1043446.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
heparin-binding protein
azurocidin
cationic antibacterial protein 37kDa (CAP37)
Opis:
Azurocidin, also known as cationic antimicrobial protein 37 kDa (CAP37) or heparin-binding protein (HBP) is an inactive homolog of serine proteinases residing in granulocytes. The ability to cleave peptide bond was lost due to replacement of two of the three residues from the conserved catalytic triad characteristic for serine proteinases. Azurocidin has a broad spectrum of antimicrobial activity, mainly against Gram-negative bacteria. It is also recognized as a multifunctional inflammatory mediator for its contracting effects on endothelial cells causing an increase of vascular permeability, capacity to bind endotoxin and ability to attract monocytes to inflammation sites.
Źródło:
Acta Biochimica Polonica; 2003, 50, 3; 743-752
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Catalytic activity of mutants of yeast protein kinase CK2α
Autorzy:
Sajnaga, Ewa
Kubiński, Konrad
Szyszka, Ryszard
Powiązania:
https://bibliotekanauki.pl/articles/1040685.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protein phosphorylation
ATP binding
mutagenesis
protein kinase CK2
ATP-competitive inhibitors
Saccharomyces cerevisiae
spermine
heparin
yeast
Opis:
Yeast CK2 is a highly conserved member of the protein kinase CGMC subfamily composed of two catalytic (α and α') and two regulatory (β and β') subunits. The amino-acid sequences of both catalytic subunits are only 60% homologous. Modelling of the tertiary structure of the CK2α displays additional α-helical structures not present in the CK2α' subunit, connecting the ATP-binding loop with the catalytic and activation loops. Deletion of this part causes drastic structural and enzymatic changes of the protein (CK2αΔ91-128) with characteristics similar to yeast CK2α' (low sensitivity to salt, heparin and spermine). Additionally, the deletion causes an over 5-fold decrease of the binding affinity for ATP and ATP-competitive inhibitors (TBBt and TBBz). The structural basis for TBBt and TBBz selectivity is provided by the hydrophobic pocket adjacent to the ATP/GTP binding site, which is smaller in CK2 than in the majority of other protein kinases. The importance of hydrophobic interactions in the binding of specific inhibitors was investigated here by mutational analysis of CK2α residues whose side chains contribute to reducing the size of the hydrophobic pocket. Site-directed mutagenesis was used to replace Val67 and Ile213 by Ala. The kinetic properties of the single mutants CK2αVal67Ala and CK2αIle213Ala, and the double mutant CK2Val67Ala Ile213Ala were studied with respect to ATP, and both inhibitors TBBt and TBBz. The Km values for ATP did not change or were very close to those of the parental kinase. In contrast, all CK2α mutants analysed displayed higher Ki values towards the inhibitors (10 to 12-fold higher with TBBt and 3 to 6-fold with TBBt) comparing to recombinant wild-type CK2α.
Źródło:
Acta Biochimica Polonica; 2008, 55, 4; 767-776
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

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