1URF

HR1b domain from PRK1

1URF の概要

• エントリーDOI: 10.2210/pdb1urf/pdb
• 関連するPDBエントリー: 1CXZ
• 分子名称: PROTEIN KINASE C-LIKE 1 (1 entity in total)
• 機能のキーワード: transferase, g-protein, hr1 domain, kinase, helical, coiled coil, atp-binding, serine/threonine-protein kinase, phosphorylation
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm: Q16512
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9017.42

構造登録者

Owen, D.,Lowe, P.N.,Nietlispach, D.,Brosnan, C.E.,Chirgadze, D.Y.,Parker, P.J.,Blundell, T.L.,Mott, H.R. (登録日: 2003-10-29, 公開日: 2003-11-06, 最終更新日: 2024-05-15)

主引用文献

Owen, D.,Lowe, P.N.,Nietlispach, D.,Brosnan, C.E.,Chirgadze, D.Y.,Parker, P.J.,Blundell, T.L.,Mott, H.R.
Molecular Dissection of the Interaction between the Small G Proteins Rac1 and Rhoa and Protein Kinase C-Related Kinase 1 (Prk1)
J.Biol.Chem., 278:50578-, 2003

PubMed Abstract: PRK1 is a serine/threonine kinase that belongs to the protein kinase C superfamily. It can be activated either by members of the Rho family of small G proteins, by proteolysis, or by interaction with lipids. Here we investigate the binding of PRK1 to RhoA and Rac1, two members of the Rho family. We demonstrate that PRK1 binds with a similar affinity to RhoA and Rac1. We present the solution structure of the second HR1 domain from the regulatory N-terminal region of PRK1, and we show that it forms an anti-parallel coiled-coil. In addition, we have used NMR to map the binding contacts of the HR1b domain with Rac1. These are compared with the contacts known to form between HR1a and RhoA. We have used mutagenesis to define the residues in Rac that are important for binding to HR1b. Surprisingly, as well as residues adjacent to Switch I, in Switch II, and in helix alpha5, it appears that the C-terminal stretch of basic amino acids in Rac is required for a high affinity interaction with HR1b.

PubMed: 14514689
DOI: 10.1074/JBC.M304313200

実験手法

SOLUTION NMR