7B51

Crystal structure of human CRM1 covalently modified by 2-mercaptoethanol at Cys528

Summary for 7B51

• Entry DOI: 10.2210/pdb7b51/pdb
• Descriptor: GTP-binding nuclear protein Ran, Exportin-1, GUANOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: exportin, inhibition, nuclear protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 143374.38

Authors

Shaikhqasem, A.,Ficner, R. (deposition date: 2020-12-03, release date: 2021-03-10, Last modification date: 2024-01-31)

Primary citation

Shaikhqasem, A.,Schmitt, K.,Valerius, O.,Ficner, R.
Crystal structure of human CRM1, covalently modified by 2-mercaptoethanol on Cys528, in complex with RanGTP.
Acta Crystallogr.,Sect.F, 77:70-78, 2021

PubMed Abstract: 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.

PubMed: 33682791
DOI: 10.1107/S2053230X2100203X

Experimental method

X-RAY DIFFRACTION (2.58 Å)