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Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria.. De plus, nous expédions HSCB Anticorps (20) et HSCB Kits (4) et beaucoup plus de produits pour cette protéine.
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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 (Montrer CDH2 Protéines) 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 (Montrer NFS1 Protéines) binds preferentially to the D-state of ISCU (Montrer ISCU Protéines) while mtHSP70 (Montrer HSPA9 Protéines) binds preferentially to the D-state of ISCU (Montrer ISCU Protéines) and HSC20 binds preferentially to the S-state of ISCU (Montrer ISCU Protéines).
A cysteine-rich N-terminal domain, which clearly distinguishes hHSC20 from the specialized DnaJ (Montrer DNAJB6 Protéines) 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