1GUA

HUMAN RAP1A, RESIDUES 1-167, DOUBLE MUTANT (E30D,K31E) COMPLEXED WITH GPPNHP AND THE RAS-BINDING-DOMAIN OF HUMAN C-RAF1, RESIDUES 51-131

1GUA の概要

• エントリーDOI: 10.2210/pdb1gua/pdb
• 分子名称: RAP1A, C-RAF1, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: oncogene protein/kinase/effector protein gtp-binding-protein, complex (gtp-binding-atp-binding), complex (gtp-binding-atp-binding) complex, complex (gtp-binding/atp-binding)
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell membrane; Lipid-anchor: P62834; Cytoplasm (By similarity): P04049
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28831.89

構造登録者

Nassar, N.,Wittinghofer, A. (登録日: 1996-06-18, 公開日: 1997-01-11, 最終更新日: 2024-02-07)

主引用文献

Nassar, N.,Horn, G.,Herrmann, C.,Block, C.,Janknecht, R.,Wittinghofer, A.
Ras/Rap effector specificity determined by charge reversal.
Nat.Struct.Biol., 3:723-729, 1996

PubMed Abstract: Members of the Ras subfamily of small GTP-binding proteins have been shown to be promiscuous towards a variety of putative effector molecules such as the protein kinase c-Raf and the Ral-specific guanine nucleotide exchange factor (Ral-GEF). To address the question of specificity of interactions we have introduced the mutations E30D and K31E into Rap and show biochemically, by X-ray structure analysis and by transfection in vivo that the identical core effector region of Ras and Rap (residues 32-40) is responsible for molecular recognition, but that residues outside this region are responsible for the specificity of the interaction. The major determinant for the switch in specificity is the opposite charge of residue 31--Lys in Rap, Glu in Ras--which creates a favourable complementary interface for the Ras-Raf interaction.

PubMed: 8756332
DOI: 10.1038/nsb0896-723

実験手法

X-RAY DIFFRACTION (2 Å)