1I35

SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF THE PROTEIN KINASE BYR2 FROM SCHIZOSACCHAROMYCES POMBE

1I35 の概要

• エントリーDOI: 10.2210/pdb1i35/pdb
• 分子名称: PROTEIN KINASE BYR2 (1 entity in total)
• 機能のキーワード: ubiquitin superfold, transferase
• 由来する生物種: Schizosaccharomyces pombe (fission yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10987.69

構造登録者

Gronwald, W.,Huber, F.,Grunewald, P.,Sporner, M.,Wohlgemuth, S.,Herrmann, C.,Kalbitzer, H.R. (登録日: 2001-02-13, 公開日: 2001-12-12, 最終更新日: 2024-05-22)

主引用文献

Gronwald, W.,Huber, F.,Grunewald, P.,Sporner, M.,Wohlgemuth, S.,Herrmann, C.,Kalbitzer, H.R.
Solution structure of the Ras binding domain of the protein kinase Byr2 from Schizosaccharomyces pombe.
Structure, 9:1029-1041, 2001

PubMed Abstract: After activation, small GTPases such as Ras transfer the incoming signal to effectors by specifically interacting with the binding domain of these proteins. Structural details of the binding domain of different effectors determine which pathway is predominantly activated. Byr2 from fission yeast is a functional homolog of Raf, which is the direct downstream target of Ras in mammalians that initiates a protein kinase cascade. The amino acid sequence of Byr2's Ras binding domain is only weakly related to that of Raf, and Byr2's three-dimensional structure is unknown.

PubMed: 11709167
DOI: 10.1016/S0969-2126(01)00671-2

実験手法

SOLUTION NMR