2P6B

Crystal Structure of Human Calcineurin in Complex with PVIVIT Peptide

2P6B の概要

• エントリーDOI: 10.2210/pdb2p6b/pdb
• 分子名称: PVIVIT 14-mer Peptide, Calmodulin-dependent calcineurin A subunit alpha isoform, Calcineurin subunit B isoform 1, ... (8 entities in total)
• 機能のキーワード: beta-sheet augmentation; protein-peptide complex, hydrolase-hydrolase regulator complex, hydrolase/hydrolase regulator
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 125727.47

構造登録者

Li, H.,Zhang, L.,Rao, A.,Harrison, S.C.,Hogan, P.G. (登録日: 2007-03-16, 公開日: 2007-06-05, 最終更新日: 2024-10-30)

主引用文献

Li, H.,Zhang, L.,Rao, A.,Harrison, S.C.,Hogan, P.G.
Structure of calcineurin in complex with PVIVIT peptide: Portrait of a low-affinity signalling interaction
J.Mol.Biol., 369:1296-1306, 2007

PubMed Abstract: The protein phosphatase calcineurin recognizes a wide assortment of substrates and controls diverse developmental and physiological pathways in eukaryotic cells. Dephosphorylation of the transcription factor NFAT and certain other calcineurin substrates depends on docking of calcineurin at a PxIxIT consensus site. We describe here the structural basis for recognition of the PxIxIT sequence by calcineurin. We demonstrate that the high-affinity peptide ligand PVIVIT adds as a beta-strand to the edge of a beta-sheet of calcineurin; that short peptide segments containing the PxIxIT consensus sequence suffice for calcineurin-substrate docking; and that sequence variations within the PxIxIT core modulate the K(d) of the interaction within the physiological range 1 microM to 1 mM. Calcineurin can adapt to a wide variety of substrates, because recognition requires only a PxIxIT sequence and because variation within the core PxIxIT sequence can fine-tune the affinity to match the physiological signalling requirements of individual substrates.

PubMed: 17498738
DOI: 10.1016/j.jmb.2007.04.032

実験手法

X-RAY DIFFRACTION (2.3 Å)