Title : Crystal structure of human CRM1, covalently modified by 2-mercaptoethanol on Cys528, in complex with RanGTP.

Pub. Date : 2021 Mar 1

PMID : 33682791






1 Functional Relationships(s)
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1 Structural analysis of several inhibitor compounds bound to CRM1 revealed that their mechanism of action relies on the covalent modification of a critical cysteine residue (Cys528 in the human receptor) located in the nuclear export signal-binding cleft. Cysteine exportin 1 Homo sapiens