4GQB

Crystal Structure of the human PRMT5:MEP50 Complex

4GQB の概要

• エントリーDOI: 10.2210/pdb4gqb/pdb
• 分子名称: Protein arginine N-methyltransferase 5, Methylosome protein 50, Histone H4 peptide, ... (5 entities in total)
• 機能のキーワード: tim barrel, beta-propeller, methyltransferase, methylation, transferase-protein binding complex, transferase/protein binding
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 112155.91

構造登録者

Antonysamy, S.,Bonday, Z.,Campbell, R.,Doyle, B.,Druzina, Z.,Gheyi, T.,Han, B.,Jungheim, L.N.,Qian, Y.,Rauch, C.,Russell, M.,Sauder, J.M.,Wasserman, S.R.,Weichert, K.,Willard, F.S.,Zhang, A.,Emtage, S. (登録日: 2012-08-22, 公開日: 2012-10-17, 最終更新日: 2024-10-16)

主引用文献

Antonysamy, S.,Bonday, Z.,Campbell, R.M.,Doyle, B.,Druzina, Z.,Gheyi, T.,Han, B.,Jungheim, L.N.,Qian, Y.,Rauch, C.,Russell, M.,Sauder, J.M.,Wasserman, S.R.,Weichert, K.,Willard, F.S.,Zhang, A.,Emtage, S.
Crystal structure of the human PRMT5:MEP50 complex.
Proc.Natl.Acad.Sci.USA, 109:17960-17965, 2012

PubMed Abstract: Protein arginine methyltransferases (PRMTs) play important roles in several cellular processes, including signaling, gene regulation, and transport of proteins and nucleic acids, to impact growth, differentiation, proliferation, and development. PRMT5 symmetrically di-methylates the two-terminal ω-guanidino nitrogens of arginine residues on substrate proteins. PRMT5 acts as part of a multimeric complex in concert with a variety of partner proteins that regulate its function and specificity. A core component of these complexes is the WD40 protein MEP50/WDR77/p44, which mediates interactions with binding partners and substrates. We have determined the crystal structure of human PRMT5 in complex with MEP50 (methylosome protein 50), bound to an S-adenosylmethionine analog and a peptide substrate derived from histone H4. The structure of the surprising hetero-octameric complex reveals the close interaction between the seven-bladed β-propeller MEP50 and the N-terminal domain of PRMT5, and delineates the structural elements of substrate recognition.

PubMed: 23071334
DOI: 10.1073/pnas.1209814109

実験手法

X-RAY DIFFRACTION (2.06 Å)