Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl
Preferences help
Polish version English version Language
enabled [disable] Abstract
Number of results

Results found: 4

Number of results on page
first rewind previous Page / 1 next fast forward last

Search results

help Sort By:

help Limit search:
first rewind previous Page / 1 next fast forward last
1
Content available remote

Interaction of class A G protein-coupled receptors with G protein.

100%
Ślusarz R., Ciarkowski J.
|
EN
A model for interaction of class A G protein-coupled receptor with the G protein Gα subunit is proposed using the rhodopsin-transducin (RD/Gt) prototype. The model combines the resolved interactions/distances, essential in the active RD*/Gt system, with the structure of Gtα C-terminal peptide bound to RD* while stabilizing it. Assuming the interactions involve conserved parts of the partners, the model specifies the conserved Helix 2 non-polar X- - -X, Helix 3 DRY and Helix 7/8 NP- -Y- - F RD* motifs interacting with the Gtα C-terminal peptide, in compliance with the structure of the latter. A concomitant role of Gtα and Gtγ>C-termini in stabilizing RD* could possibly be resolved assuming a receptor dimer as requisite for G protein activation.
2
Content available remote

Conformational changes of peptidoglycan fragments during their interactions with vancomycin

81%
Ślusarz R., Ślusarz M., Samaszko J., Madaj J.
Open Chemistry
|
2011
|
vol. 9
|
issue 3
422-431
EN
Six complexes of vancomycin and peptidoglycan precursors were studied via molecular dynamics simulations. The interactions between the antibiotic and peptidoglycan fragments were identified and described in detail. All six studied modifications of the peptidoglycan precursor resulted in a weakening of the interaction with vancomycin when comparing to the native D-Ala-D-Ala-terminated fragment. It was confirmed that the N-terminus of the vancomycin is directly responsible for peptidoglycan recognition and antimicrobial activity. In simulated systems, the saccharide part of the antibiotic interacts with peptide precursors, thus it could also be important for antimicrobial activity. The complex terminated with D-Lac is the only one in which there is a weak interaction with the sugar moiety in the simulated systems. Analysis of conformational changes is a major scope of this work. The lack of interactions resulting from modification of the peptidoglycan precursors (D-Lac, D-Ser or other substitution) would be counterbalanced by proper modifications of the vancomycin moiety, especially the saccharide part of vancomycin.
3
Content available remote

Signal transmission via G protein-coupled receptors in the light of rhodopsin structure determination.

71%
Ciarkowski J., Drabik P., Giełdoń A., Kaźmierkiewicz R., Ślusarz R.
|
2001
|
vol. 48
|
issue 4
1203-1207
EN
G protein-coupled receptors (GPCRs) transducing diverse external signals to cells via activation of heterotrimeric GTP-binding (G) proteins, estimated to mediate actions of 60% of drugs, had been resistant to structure determination until summer 2000. The first atomic-resolution experimental structure of a GPCR, that of dark (inactive) rhodopsin, thus provides a trustworthy 3D prototype for antagonist-bound forms of this huge family of proteins. In this work, our former theoretical GPCR models are evaluated against the new experimental template. Subsequently, a working hypothesis regarding the signal transduction mechanism by GPCRs is presented.
4
Content available remote

Molecular docking-based test for affinities of two ligands toward vasopressin and oxytocin receptors.

71%
Ślusarz R., Kaźmierkiewicz R., Giełdoń A., Lammek B., Ciarkowski J.
|
2001
|
vol. 48
|
issue 1
131-135
EN
Molecular docking simulations are now fast developing area of research. In this work we describe an effective procedure of preparation of the receptor-ligand complexes. The amino-acid residues involved in ligand binding were identified and described.
first rewind previous Page / 1 next fast forward last
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.