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7b51
From Proteopedia
Crystal structure of human CRM1 covalently modified by 2-mercaptoethanol at Cys528
Structural highlights
FunctionRAN_HUMAN GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2.[1] [2] [3] [4] Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.[5] [6] [7] [8] Publication Abstract from PubMedCRM1 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 A resolution. The results demonstrate that buffer components can interfere with the characterization of cysteine-dependent inhibitor compounds. Crystal structure of human CRM1, covalently modified by 2-mercaptoethanol on Cys528, in complex with RanGTP.,Shaikhqasem A, Schmitt K, Valerius O, Ficner R Acta Crystallogr F Struct Biol Commun. 2021 Mar 1;77(Pt 3):70-78. doi: , 10.1107/S2053230X2100203X. Epub 2021 Mar 3. PMID:33682791[9] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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