Tudor domain

A Tudor domain is a conserved protein domain that was originally identified as a 50 amino acid region in the Drosophila Tudor protein . The corresponding, structurally characterized Tudor domain in the human SMN protein (SMN = survival of motor neuron) consists of 5 anti-parallel β-sheets with a barrel-like fold. This domain recognizes symmetrically methylated arginine .

The proteins TP53BP1 (Tumor suppressor p53-binding protein 1) and its homolog in the fission yeast Crb2 and JMJD2A (Jumonji domain containing 2A) contain either tandem or double Tudor domains and recognize methylated histones .

Tudor domains have also been found to play a role in RNA binding. The structural basis of ligand binding is not yet understood. Other Tudor domain proteins are AKAP1 (A-kinase anchor protein 1) and ARID4A (AT rich interactive domain 4A) and others.

literature

↑ Remco Sprangers, Matthew R. Groves, Irmgard Sinning and Michael Sattler: High-resolution X-ray and NMR Structures of the SMN Tudor Domain: Conformational Variation in the Binding Site for Symmetrically Dimethylated Arginine Residues . In: Journal of Molecular Biology . 327, No. 2, pp. 507-520. doi : 10.1016 / S0022-2836 (03) 00148-7 .
↑ Botuyan MV, Lee J, Ward IM, Kim JE, Thompson JR, Chen J, Mer G: Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. . In: Cell . 127, No. 7, pp. 1361-1373. doi : 10.1016 / j.cell.2006.10.043 .
↑ Huang Y, Fang J, Bedford MT, Zhang Y, Xu RM: Recognition of Histone H3 Lysine-4 Methylation by the Double Tudor Domain of JMJD2A . In: Science . 312, No. 5774, pp. 748-751. doi : 10.1126 / science.1125162 .
↑ Lee J, Thompson JR, Botuyan MV, Mer G: Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor . In: Nature Structural & Molecular Biology . 15, No. 1, pp. 109-111. doi : 10.1038 / nsmb1326 .
↑ Rogne M, Landsverk HB, Van Eynde A, Beullens M, Bollen M, Collas P, Küntziger T: The KH-Tudor Domain of A-Kinase Anchoring Protein 149 Mediates RNA-Dependent Self-Association . In: Biochemistry . 45, No. 50, pp. 14980-14989. doi : 10.1021 / bi061418y .

[1] Remco Sprangers, Matthew R. Groves, Irmgard Sinning and Michael Sattler: High-resolution X-ray and NMR Structures of the SMN Tudor Domain: Conformational Variation in the Binding Site for Symmetrically Dimethylated Arginine Residues . In: Journal of Molecular Biology . 327, No. 2, pp. 507-520. doi : 10.1016 / S0022-2836 (03) 00148-7 .

[2] Botuyan MV, Lee J, Ward IM, Kim JE, Thompson JR, Chen J, Mer G: Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. . In: Cell . 127, No. 7, pp. 1361-1373. doi : 10.1016 / j.cell.2006.10.043 .

[3] Huang Y, Fang J, Bedford MT, Zhang Y, Xu RM: Recognition of Histone H3 Lysine-4 Methylation by the Double Tudor Domain of JMJD2A . In: Science . 312, No. 5774, pp. 748-751. doi : 10.1126 / science.1125162 .

[4] Lee J, Thompson JR, Botuyan MV, Mer G: Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor . In: Nature Structural & Molecular Biology . 15, No. 1, pp. 109-111. doi : 10.1038 / nsmb1326 .

[5] Rogne M, Landsverk HB, Van Eynde A, Beullens M, Bollen M, Collas P, Küntziger T: The KH-Tudor Domain of A-Kinase Anchoring Protein 149 Mediates RNA-Dependent Self-Association . In: Biochemistry . 45, No. 50, pp. 14980-14989. doi : 10.1021 / bi061418y .