5MYC

Crystal structure of human 14-3-3 sigma in complex with LRRK2 peptide pS910

5MYC の概要

• エントリーDOI: 10.2210/pdb5myc/pdb
• 分子名称: 14-3-3 protein sigma, Leucine-rich repeat serine/threonine-protein kinase 2, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: 14-3-3 lrrk2 phosphorylation ppi, transferase
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Cytoplasm: P31947; Membrane; Peripheral membrane protein: Q5S007
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31140.33

構造登録者

Stevers, L.M.,de Vries, R.M.J.M.,Ottmann, C. (登録日: 2017-01-26, 公開日: 2017-03-01, 最終更新日: 2024-11-06)

主引用文献

Stevers, L.M.,de Vries, R.M.,Doveston, R.G.,Milroy, L.G.,Brunsveld, L.,Ottmann, C.
Structural interface between LRRK2 and 14-3-3 protein.
Biochem. J., 474:1273-1287, 2017

PubMed Abstract: Binding of 14-3-3 proteins to leucine-rich repeat protein kinase 2 (LRRK2) is known to be impaired by many Parkinson's disease (PD)-relevant mutations. Abrogation of this interaction is connected to enhanced LRRK2 kinase activity, which in turn is implicated in increased ubiquitination of LRRK2, accumulation of LRRK2 into inclusion bodies and reduction in neurite length. Hence, the interaction between 14-3-3 and LRRK2 is of significant interest as a possible drug target for the treatment of PD. However, LRRK2 possesses multiple sites that, upon phosphorylation, can bind to 14-3-3, thus rendering the interaction relatively complex. Using biochemical assays and crystal structures, we characterize the multivalent interaction between these two proteins.

PubMed: 28202711
DOI: 10.1042/BCJ20161078

実験手法

X-RAY DIFFRACTION (1.459 Å)