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Wyszukujesz frazę "PDZ domain" wg kryterium: Wszystkie pola


Wyświetlanie 1-3 z 3
Tytuł:
PDZ domains - common players in the cell signaling.
Autorzy:
Jeleń, Filip
Oleksy, Arkadiusz
Śmietana, Katarzyna
Otlewski, Jacek
Powiązania:
https://bibliotekanauki.pl/articles/1043370.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
PDZ domain
module
protein-protein interaction
signaling
Opis:
PDZ domains are ubiquitous protein interaction modules that play a key role in cellular signaling. Their binding specificity involves recognition of the carboxyl-terminus of various proteins, often belonging to receptor and ion channel families. PDZ domains also mediate more complicated molecular networks through PDZ-PDZ interactions, recognition of internal protein sequences or phosphatidylinositol moieties. The domains often form a tandem of multiple copies, but equally often such tandems or single PDZ domain occur in combination with other signaling domains (for example SH3, DH/PH, GUK, LIM, CaMK). Common occurrence of PDZ domains in Metazoans strongly suggests that their evolutionary appearance results from the complication of signaling mechanisms in multicellular organisms. Here, we focus on their structure, specificity and role in signaling pathways.
Źródło:
Acta Biochimica Polonica; 2003, 50, 4; 985-1017
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Degenerate specificity of PDZ domains from RhoA-specific nucleotide exchange factors PDZRhoGEF and LARG
Autorzy:
Smietana, Katarzyna
Kasztura, Monika
Paduch, Marcin
Derewenda, Urszula
Derewenda, Zygmunt
Otlewski, Jacek
Powiązania:
https://bibliotekanauki.pl/articles/1040739.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
binding specificity
LARG
PDZ domain
PDZRhoGEF
phage display
Opis:
PDZ domains are ubiquitous protein-protein interaction modules which bind short, usually carboxyterminal fragments of receptors, other integral or membrane-associated proteins, and occasionally cytosolic proteins. Their role in organizing multiprotein complexes at the cellular membrane is crucial for many signaling pathways, but the rules defining their binding specificity are still poorly understood and do not readily explain the observed diversity of their known binding partners. Two homologous RhoA-specific, multidomain nucleotide exchange factors PDZRhoGEF and LARG contain PDZ domains which show a particularly broad recognition profile, as suggested by the identification of five diverse biological targets. To investigate the molecular roots of this phenomenon, we constructed a phage display library of random carboxyterminal hexapeptides. Peptide variants corresponding to the sequences identified in library selection were synthesized and their affinities for both PDZ domains were measured and compared with those of peptides derived from sequences of natural partners. Based on the analysis of the binding sequences identified for PDZRhoGEF, we propose a sequence for an 'optimal' binding partner. Our results support the hypothesis that PDZ-peptide interactions may be best understood when one considers the sum of entropic and dynamic effects for each peptide as a whole entity, rather than preferences for specific residues at a given position.
Źródło:
Acta Biochimica Polonica; 2008, 55, 2; 269-280
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
AtDeg2 - a chloroplast protein with dual protease/chaperone activity
Autorzy:
Jagodzik, P.
Adamiec, M.
Jackowski, G.
Powiązania:
https://bibliotekanauki.pl/articles/57301.pdf
Data publikacji:
2014
Wydawca:
Polskie Towarzystwo Botaniczne
Tematy:
chloroplast protein
protease
proteolytic enzyme
chaperone
enzyme activity
chloroplast
PDZ domain
Opis:
Chloroplast protease AtDeg2 (an ATP-independent serine endopeptidase) is cytosolically synthesized as a precursor, which is imported into the chloroplast stroma and deprived of its transit peptide. Then the mature protein undergoes routing to its functional location at the stromal side of thylakoid membrane. In its linear structure AtDeg2 molecule contains the protease domain with catalytic triad (HDS) and two PDZ domains (PDZ1 and PDZ2). In vivo AtDeg2 most probably exists as a supposedly inactive haxamer, which may change its oligomeric stage to form active 12-mer, or 24-mer. AtDeg2 has recently been demonstrated to exhibit dual protease/chaperone function. This review is focused on the current awareness with regard to AtDeg2 structure and functional significance.
Źródło:
Acta Societatis Botanicorum Poloniae; 2014, 83, 3
0001-6977
2083-9480
Pojawia się w:
Acta Societatis Botanicorum Poloniae
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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