1V66

Solution structure of human p53 binding domain of PIAS-1

1V66 の概要

• エントリーDOI: 10.2210/pdb1v66/pdb
• NMR情報: BMRB: 6072
• 分子名称: Protein inhibitor of activated STAT protein 1 (1 entity in total)
• 機能のキーワード: four helix bundle, riken structural genomics/proteomics initiative, rsgi, structural genomics, ligase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus speckle: O75925
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7466.98

構造登録者

Okubo, S.,Hara, F.,Tsuchida, Y.,Shimotakahara, S.,Suzuki, S.,Hatanaka, H.,Yokoyama, S.,Tanaka, H.,Yasuda, H.,Shindo, H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2003-11-27, 公開日: 2004-12-07, 最終更新日: 2023-12-27)

主引用文献

Okubo, S.,Hara, F.,Tsuchida, Y.,Shimotakahara, S.,Suzuki, S.,Hatanaka, H.,Yokoyama, S.,Tanaka, H.,Yasuda, H.,Shindo, H.
NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers
J.Biol.Chem., 279:31455-31461, 2004

PubMed Abstract: A member of the PIAS (protein inhibitor of activated STAT) family of proteins, PIAS1, have been reported to serve as an E3-type SUMO ligase for tumor suppressor p53 and its own. It also was proposed that the N-terminal domain of PIAS1 interacts with DNA as well as p53. Extensive biochemical studies have been devoted recently to understand sumoylations and its biological implications, whereas the structural aspects of the PIAS family and the mechanism of its interactions with various factors are less well known to date. In this study, the three-dimensional structure of the N-terminal domain (residues 1-65) of SUMO ligase PIAS1 was determined by NMR spectroscopy. The structure revealed a unique four-helix bundle with a topology of an up-down-extended loop-down-up, a part of which the helix-extended loop-helix represented the SAP (SAF-A/B, Acinus, and PIAS) motif. Thus, this N-terminal domain may be referred to as a four-helix SAP domain. The glutathione S-transferase pull-down assay demonstrated that this domain possesses a binding ability to tumor suppressor p53, a target protein for sumoylation by PIAS1, whereas gel mobility assays showed that it has a strong affinity toward A/T-rich DNA. An NMR analysis of the four-helix SAP domain complexed with the 16-bp-long DNA demonstrated that one end of the four-helix bundle is the binding site and may fit into the minor groove of DNA. The three-dimensional structure and its binding duality are discussed in conjunction with the biological functions of PIAS1 as a SUMO ligase.

PubMed: 15133049
DOI: 10.1074/jbc.M403561200

実験手法

SOLUTION NMR