Binding affinity of the disordered C-terminal region of measles virus nucleoprotein with Hsp70

Range ~70μM: in the presence of stoichiometric amounts of the cochaperone Hsp40 ~50nM
Organism Measels virus
Reference Theillet FX et al., Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs). Chem Rev. 2014 Jul 9 114(13):6661-714. doi: 10.1021/cr400695p p.6676 right column 4th paragraphPubMed ID24901537
Primary Source [368] Marie Couturier et al., High affinity binding between Hsp70 and the C‐terminal domain of the measles virus nucleoprotein requires an Hsp40 co‐chaperone. J. Mol. Recognit. 2009, 23, 301 link
Comments P.6676 right column 4th paragraph: "Another level of complexity may involve cochaperone interactions with both IDPs [intrinsically disordered proteins], and chaperones. The disordered C-terminal region of measles virus nucleoprotein for example, binds Hsp70 with ∼70 μM affinity (primary source) In the presence of stoichiometric amounts of the cochaperone Hsp40, the dissociation constant decreases to ∼50 nM. Thus, cochaperones can modulate IDP-chaperone affinities, which may be particularly important during translation, when multiple chaperones and cochaperones line the ribosomal exit tunnel (ref 369)."
Entered by Uri M
ID 116289