4G56

Crystal Structure of full length PRMT5/MEP50 complexes from Xenopus laevis

4G56 の概要

• エントリーDOI: 10.2210/pdb4g56/pdb
• 分子名称: Hsl7 protein, MGC81050 protein, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total)
• 機能のキーワード: protein arginine methyltransferase, protein complexes, histone methylation, transferase, structural genomics, psi-biology, new york structural genomics research consortium, nysgrc
• 由来する生物種: Xenopus laevis (clawed frog,common platanna,platanna); 詳細
• 細胞内の位置: Cytoplasm: Q6NUA1 Q6NUD0
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 229941.22

構造登録者

Ho, M.,Wilczek, C.,Bonanno, J.,Shechter, D.,Almo, S.C.,New York Structural Genomics Research Consortium (NYSGRC) (登録日: 2012-07-17, 公開日: 2012-10-03, 最終更新日: 2017-11-15)

• 主引用文献: Ho, M.C.,Wilczek, C.,Bonanno, J.B.,Xing, L.,Seznec, J.,Matsui, T.,Carter, L.G.,Onikubo, T.,Kumar, P.R.,Chan, M.K.,Brenowitz, M.,Cheng, R.H.,Reimer, U.,Almo, S.C.,Shechter, D.; Structure of the arginine methyltransferase PRMT5-MEP50 reveals a mechanism for substrate specificity; Plos One, 8:e57008-e57008, 2013; PubMed: 23451136; DOI: 10.1371/journal.pone.0057008

実験手法

X-RAY DIFFRACTION (2.95 Å)