The dynamic configuration and phosphorylation of the C-terminal HEAT domain of huntingtin modulates its function

ABSTRACT: Chemical cross-linking coupled to mass spectrometry was used to study different forms of human huntingtin (HTT). The variants included wild-type protein with poly-Q tail lengths of 23 and 78 and Ser2116 > Ala mutation of Q23- and Q78-HTT. Cross-linking was performed using the homobifunctional, lysine-reactive disuccinimidyl suberate (DSS).

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

DISEASE(S): Huntington Disease

SUBMITTER: Alexander Leitner  

LAB HEAD: Ji-Joon Song

PROVIDER: PXD013907 | Pride | 2020-07-07

REPOSITORIES: Pride