TY  - JOUR
A1  - Shaikhqasem, Alaa
A1  - Schmitt, Kerstin
A1  - Valerius, Oliver
A1  - Ficner, Ralf
T1  - Crystal structure of human CRM1, covalently modified by 2‐mercaptoethanol on Cys528, in complex with RanGTP
Y1  - 2021-03-08
VL  - 77
IS  - 3
SP  - 70
EP  - 78
JF  - Acta Crystallographica Section F
DO  - 10.23689/fidgeo-4314
PB  - International Union of Crystallography
N2  - CRM1 is a nuclear export receptor that has been intensively targeted over the last decade for the development of antitumor and antiviral drugs. 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. This study presents the crystal structure of human CRM1, covalently modified by 2‐mercaptoethanol on Cys528, in complex with RanGTP at 2.58 Å resolution. The results demonstrate that buffer components can interfere with the characterization of cysteine‐dependent inhibitor compounds.
N2  - The covalent modification of human CRM1 by 2‐mercaptoethanol interferes with the characterization of cysteine‐dependent inhibitor compounds. image
UR  - http://resolver.sub.uni-goettingen.de/purl?gldocs-11858/8660
ER  -