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Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria.. Zusätzlich bieten wir Ihnen HSCB Antikörper (20) und HSCB Kits (4) und viele weitere Produktgruppen zu diesem Protein an.
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The delivery of assembled Fe-S clusters to recipient proteins is a crucial step in the biogenesis of Fe-S proteins; review focuses on recent insights into the molecular mechanism of amino acid motif recognition and discrimination by the co-chaperone HSC20 and finds co-chaperone HSC20 binds to LYR (zeige CDH2 Proteine) motifs present in Fe-S recipient proteins or their binding partners. [Review]
the crucial role of HSC20 in the assembly of the mitochondrial respiratory chain, is reported.
NFS1 (zeige NFS1 Proteine) binds preferentially to the D-state of ISCU (zeige ISCU Proteine) while mtHSP70 (zeige HSPA9 Proteine) binds preferentially to the D-state of ISCU (zeige ISCU Proteine) and HSC20 binds preferentially to the S-state of ISCU (zeige ISCU Proteine).
A cysteine-rich N-terminal domain, which clearly distinguishes hHSC20 from the specialized DnaJ (zeige DNAJB6 Proteine) type III proteins of fungi and most bacteria, was found to be important for the integrity and function of the human co-chaperone.
structural analysis of human J-type co-chaperone HscB reveals a tetracysteine metal-binding domain
Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria.
iron-sulfur cluster co-chaperone protein HscB, mitochondrial
, HscB iron-sulfur cluster co-chaperone homolog (E. coli)
, J-type co-chaperone HSC20
, DnaJ (Hsp40) homolog, subfamily C, member 20
, dnaJ homolog subfamily C member 20