Английская Википедия:APAF1

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Версия от 04:07, 27 декабря 2023; EducationBot (обсуждение | вклад) (Новая страница: «{{Английская Википедия/Панель перехода}} {{Short description|Mammalian protein found in Homo sapiens}} {{Infobox_gene}} '''Apoptotic protease activating factor 1''', also known as '''APAF1''', is a human homolog of ''C. elegans'' CED-4 gene.<ref name="entrez"/><ref name="pmid9267021">{{cite journal | vauthors = Zou H, Henzel WJ, Liu X, Lutschg A, Wang X | title = Apaf-1, a human protein homologous to C. elegans CED-4, partici...»)
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Шаблон:Short description Шаблон:Infobox gene Apoptotic protease activating factor 1, also known as APAF1, is a human homolog of C. elegans CED-4 gene.[1][2][3]

Function

The protein was identified in the laboratory of Xiaodong Wang as an activator of caspase-3 in the presence of cytochromeC and dATP.[4] This gene encodes a cytoplasmic protein that forms one of the central hubs in the apoptosis regulatory network. This protein contains (from the N terminal) a caspase recruitment domain (CARD), an ATPase domain (NB-ARC), few short helical domains and then several copies of the WD40 repeat domain. Upon binding cytochrome c and dATP, this protein forms an oligomeric apoptosome. The apoptosome binds and cleaves Procaspase-9 protein, releasing its mature, activated form. The precise mechanism for this reaction is still debated though work published by Guy Salvesen suggests that the apoptosome may induce caspase-9 dimerization and subsequent autocatalysis.[5] Activated caspase-9 stimulates the subsequent caspase cascade that commits the cell to apoptosis.

Alternative splicing results in several transcript variants encoding different isoforms.[1]

Structure

APAF1 contains a CARD domain with a Greek key motif composed of six helices, a Rossman fold nucleotide binding domains, a short helical motif and a winged-helix domain.[6]

Apoptosome complex structure

Interactions

APAF1 has been shown to interact with:

References

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External links

Further reading

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